The Battle for the Soul of Smith College

The following letter to the Smith college newspaper “The Sophian” appeared in the current issue. Disclaimer: our neice went there, I’ve played chamber music with one of the Physics profs there, I’m currently studying a math book with an emeritus Smith prof who wrote it, I’ve audited a course there, I may take piano lessons from a retired music prof there. It’s a great institution with plenty of intelligent articulate undergraduates. Wendy Kaminer is a Smith Alumna. It will be fascinating to see how this plays out.

Chris Pyle

Mount Holyoke Professor

Thanks to The Sophian for publishing a transcript of what Wendy Kaminer actually said in New York. Now it is perfectly clear she is not a racist, but used the “n-word,” unexpurgated, to make a point about those caring souls who, in their effort to protect the sensibilities of students, violate free speech. The hyperventilating that followed Kaminer’s uncensored prose proves her point conclusively.

Imagine that Mark Twain had been invited to read some of his writings on campus, but that Kaminer’s critics discovered that he had used the “n-word” liberally in “The Adventures of Huckleberry Finn.” What should the college do? Disinvite him? Ask him to tone down his remarks because they might traumatize someone? Post “trigger warnings” all over campus?

The Sophian would publish Twain’s speech, but post warnings, like those that preceded the Kaminer transcript, declaring that “This author is guilty of ‘racism/racial slurs, sexist/misogynist slurs,’ and writes about ‘race-based violence.’” Twain’s admirers might be offended by such prissiness, but that’s too bad. The Sophian has a moral duty to give its adult readers early warning of impending isms on it pages. Otherwise they might be shocked, like little children confronted by age-inappropriate messages.

Unnoticed in last month’s kerfuffle was Kaminer’s provocative suggestion: “colleges and universities should . . . fire almost all of the student life administrators.” Why? Because they are the primary source of the patronizing idea that college students, especially women, are psychologically delicate souls, easily wounded by unvarnished prose. It is the duty of student life deans to create “safe spaces” for all students, free from words and ideas that might traumatize them (or anyone else).

These deans are direct descendants of Harriet Bowdler, the Victorian lady who persuaded her brother John, a publisher, to sanitize the great books so that they would be suitable for the fragile sensibilities of women and servants. As a result, it wasn’t until the 1950s that professors could find an unexpurgated edition of Shakespeare’s plays to assign to their students.

Kaminer is not the only critic of these well-meaning deans. The American Association of University Professors rejects the “presumption that students need to be protected rather than challenged” is both “infantilizing and anti-intellectual.” The American Library Association, the Foundation for Individual Rights in Education and the American Civil Liberties Union oppose content warnings for much the same reason that Smith professors once opposed Joe McCarthy’s censors who, when they weren’t removing books from libraries, stamped them with warning labels.

“When labeling is an attempt to prejudice attitudes,” the AAUP warns, it is a censor’s tool…If ‘The House of Mirth’ or ‘Anna Karenina’ carried a warning about suicide, students might overlook the other questions about wealth, love, deception and existential anxiety that are what those books are actually about.” The AAUP additionally says, “Trigger warnings also signal an expected response to the content (e.g. dismay, distress, disapproval) and eliminate the element of surprise and spontaneity that can enrich the reading experience and provide critical insight.”

When President McCartney’s committee meets, it will struggle over nothing less than the soul of the college. Will Smith continue to be a liberal arts college for strong women, or will it become a therapeutic shelter for the easily offended?

Professor Chris Pyle

It

Paul Schleyer 1930 – 2014, A remembrance

Thanks Peter for your stories and thoughts about Dr. Schleyer (I never had the temerity to even think of him as Paul). Hopefully budding chemists will read it, so they realize that even department chairs and full profs were once cowed undergraduates.

He was a marvelous undergraduate advisor, only 7 years out from his own Princeton degree when we first came in contact with him and a formidable physical and intellectual presence even then. His favorite opera recording, which he somehow found a way to get into the lab, was don Giovanni’s scream as he realized he was to descend into Hell. I never had the courage to ask him if the scars on his face were from dueling.

We’d work late in the lab, then go out for pizza. In later years, I ran into a few Merck chemists who found him a marvelous consultant. However, back in the 50’s, we’d be working late, and he’d make some crack about industrial chemists being at home whole we were working, the high point of their day being mowing their lawn.

I particularly enjoyed reading his papers when they came out in Science. To my mind he finally settled things about the nonclassical nature of the norbornyl cation — here it is, with the crusher being the very long C – C bond lengths

Science vol. 341 pp. 62 – 64 ’13 contains a truly definitive answer (hopefully) along with a lot of historical background should you be interested. An Xray crystallographic structure of a norbornyl cation (complexed with a Al2Br7- anion) at 40 Kelvin shows symmetrical disposition of the 3 carbons of the nonclassical cation. It was tricky, because the cation is so symmetric that it rotates within crystals at higher temperatures. The bond lengths between the 3 carbons are 1.78 to 1.83 Angstroms — far longer than the classic length of 1.54 Angstroms of a C – C single bond.

I earlier wrote a post on why I don’t read novels, the coincidences being so extreme that if you put them in a novel, no one would believe them and throw away the book — it involves the Princeton chemistry department and my later field of neurology — here’s the link http://luysii.wordpress.com/2014/11/13/its-why-i-dont-read-novels/

Here’s yet another. Who would have thought, that years later I’d be using a molecule Paul had synthesized to treat Parkinson’s disease as a neurologist. He did an incredibly elegant synthesis of adamantane using only the product of a Diels Alder reaction, hydrogenating it with a palladium catalyst and adding AlCl3. An amazing synthesis and an amazing coincidence.

As Peter noted, he was an extremely productive chemist and theoretician. He should have been elected to the National Academy of Sciences, but never was. It has been speculated that his wars with H. C. Brown made him some powerful enemies. I’ve heard through the grapevine that it rankled him greatly. But virtue is its own reward, and he had plenty of that.

R. I. P. Dr. Schleyer

Paul Schleyer (1930 – 2014) R. I. P.

This is a guest post by Peter J. Reilly, Anson Marston Distinguished Professor Emeritus, Department of Chemical and Biological Engineering, Iowa State University, fellow Schleyer undergraduate advisee Princeton 1958 – 1960, friend, and all around good guy.

I’ll follow with my own reminiscences in another post. Obits tend to be polished and bland, ‘speak no evil of the dead’ and all that, but Peter captures the flavor of what it was actually like to be Paul’s advisee and exposed to his formidable presence.

“Following are my thoughts on our undergraduate chemistry advisor at Princeton, Paul von Ragué Schleyer, who died on November 21 of this year at 84.

Paul was an amazingly prolific chemist. He started publishing in 1956, soon after he arrived at Princeton from receiving a Ph.D. at Harvard, where he studied from 1951 to 1954 after earning an A.B. from Princeton. He was still publishing at the time of his death. In fact, he had promised to deliver a book chapter over this Thanksgiving weekend. Over his latter years at Princeton, in the early 1970’s, his annual production of papers averaged the middle 20’s. He kept up the same pace at Universität Erlangen-Nürnberg in Germany from 1976 to 1992. From 1993 to 1997, when he had appointments at both Erlangen-Nürnberg and the University of Georgia, he was in the 40’s. When fully at Georgia, after 1997, he gradually slacked off, publishing only 16 papers this year. Altogether he had 1277 publications, when a really productive chemist with ready access to students and postdoctoral fellows hopes to have 200–250 in a full career.

Another way to consider Paul’s productivity is by how often his work had been cited (partly by his own later papers but mainly by the papers of others). A 1981–1997 survey reported that he was the third most cited chemist in the world. Althogether his works were cited over 75,000 times. His h-index is 126 in the Thomson Reuters Web of Science database, meaning that he had 126 publications that were cited at least 126 times, an astounding number.

I first met Paul in the fall of 1958, two years after I arrived at Princeton. I needed to find someone to supervise my junior paper, a ritual common to all Princeton undergraduates doing A.B. degrees. I had originally approached Edward Taylor, a somewhat older chemistry professor, but when I told him that I was somewhat interested in becoming a chemical engineer, he directed me to Paul. Paul was 28 at the time, but he seemed older to me (I supposed all professors did). He was tall, with dark black hair combed to the side over his forehead. He had a scar on his cheek and talked very precisely.

My father met him once and came away asking if he had been a German U-boat captain during WWII.

I must say that I spent a sizable part of the next two years being terrified of Paul. He had a laboratory in the second floor of the southwest corner of Frick Chemical Laboratory. The benches were full of glassware, to the point where it seemed hard to do any research. However, the item that spooked me the most was a cauldron full of boiling black liquid, supposedly mainly nitric acid, in which dirty glassware was submerged to be cleaned.

Paul gave me a project to research the incidence and properties of the benzyne intermediate, a short-lived benzene ring with a triple bond. This was my first exposure to research beyond short papers for classes, and I suppose that I did well enough for him to invite me to do a senior thesis with him. The topic was to determine the mechanism by which an obscure organic chemical rearranged itself. The title of the thesis that came from a year’s dogged effort was “A Study of the Cleavage Products of 2,5-Dimethyltetrahydropyran-2-Methanol”, but what I mainly made was black goop. Paul’s written comments to me started with the statement that he was sorry that the problem was so intractable, but at least he liked my writeup. I still have the thesis (and the junior paper). Back in 2007 I was contacted by the Princeton University Library, which had lost its copy. They asked if I could send them mine so that they could microfilm it, which of course I did.

I remember that at least four of us chemistry majors spent much of our senior years in a very large and empty laboratory working on our theses under Paul’s direction. I must say that the various chemicals that I worked on smelled a lot better than the ones that you dealt with. I used to take weekend dates up to the laboratory to show them where I worked, and I would open one of your very small tubules, I think containing butyl mercaptan. Its smell still permeated the room on Mondays. (Editor’s note — people used to look at their shoes when I walked into the eating club after working with n-Bu-SH or similar compounds).

Despite my lack of success on my thesis, I learned from it how to do research. My chemical engineering major professor at the University of Pennsylvania was hard to contact, so much of my doctoral dissertation was done without much supervision. Between the two experiences, I had a good foundation for my 46 years of being a chemical engineering professor, six at the University of Nebraska-Lincoln and 40 at Iowa State University after four years at DuPont in southern New Jersey.

I only saw Paul four times after leaving Princeton. The first was when I returned there for a short visit. The second time was at my 25th Princeton reunion, when one of his daughters was graduating. A third time was when he visited the Iowa State chemistry department to present a prestigious lecture. The fourth and last time was in 2005 when I visited the University of Georgia for a meeting. Paul spent about 30 minutes telling me about his latest research, of which I understood very little.

I will close with a little story. When I told Paul during my senior year that I wanted to go to graduate school in chemical engineering, he asked why I wanted to become a pipe-fitter. Probably because of my chemistry background at Princeton, my research was always chemistry- and biology-based, first in fermentations at Penn and Nebraska (with a detour to chloro- and fluorocarbons at DuPont), and then in enzymes and carbohydrates at Iowa State. I moved more and more into computation late in my career, and when Paul visited around 2002 I told him that I would be sending a manuscript to the Journal of Computational Chemistry, which he and Lou Allinger at Georgia had founded and were still editing. Being Paul, he immediately said in his deep voice that it had better be good. As it turned out, it sailed through the review process with hardly a blip, and I followed it up with a second manuscript a few years later.

So, we were fortunate to have Paul as a mentor during our formative years. He certainly wasn’t the sweetest guy, but he was brilliant, and hopefully a very small part of his brilliance rubbed off on us.”

Peter J. Reilly

How one membrane protein senses mechanical stress

Chemists (particularly organic chemists) think they’re pretty smart. So see if you can figure out how a membrane embedded ion channel opens due to mechanical stress. The answer is to be found in last week’s Nature (vol. 516 pp. 126 – 130 4 Dec ’14).

As you probably know, membrane embedded proteins get stuck there because they contain multiple alpha helices with mostly hydrophobic amino acids allowing them to snuggle up to the hydrocarbon tails of the lipids making up the lipid bilayer of the biological membrane.

The channel in question is called TRAAK, known to open in response to membrane tension. It conducts potassium ions. The voltage sensitive potassium channels have 24 transmembrane alpha helices, 6 in each of the tetramer proteins comprising it. TRAAK has only 8. As is typical of all ion channels, the helices act like staves on a barrel, shifting slightly to open the pore.

In this case, with little membrane tension, the helices separate slightly permitting a a 10 carbon tail ( CH3 – [ CH2 – CH2 – CH2 ]3 – ) to enter the barrel occluding the pore. Tension on the membrane tends decrease the packing of hydrocarbon tails of the membrane, pulling the plug out of the pore. Neat !! ! ! This is a completely different mechanism than the voltage sensing helix in the 24 transmembrane voltage sensitive potassium channels, and one that no one has predicted despite all their intelligence.

Trigger warning. This paper is by MacKinnon who won the Nobel for his work on potassium channels. He used antibodies to stabilize ion channels so they could be studied by crystallography. Take them out of the membrane and they denature. Why the warning? In his Nobel work he postulated an alpha helical hairpin paddle extending outward from the channel core into the membrane’s lipid interior. It was both hydrophobic and charged, and could move in response to transmembrane voltage changes.

This received vigorous criticism from others, who felt it was an artifact produced by the use of the antibody to stabilize the protein for crystallography.

Why the warning? Because MacKinnnon also used an antibody to stabilize TRAAK.

The whole idea of membrane tension brings up the question of just how strong van der Waals forces really are. Biochemists and molecular biologists tend to think of hydrophobic forces as primarily entropic, pushing hydrophobic parts of a protein together so water would have to exquisitely structure itself to solvate them (e.g. lowering the entropy greatly). Here however, the ‘pull’ if you wish, is due to the mutual attraction of the hydrophobic lipid side chains to each other, which I would imagine is pretty week.

I’m sure that these forces have been measured, and years ago I enjoyed reading about Langmuir’s work putting what was basically soap on a substrate, and forming a two dimensional gas which actually followed something resembling P * Area = n * R * T. So the van der Waals forces have been measured, I just don’t know what they are. Does anyone out there?

Nonetheless, some very slick (physical and organic) chemistry.

Tensors

Anyone wanting to understand the language of general relativity must eventually tackle tensors. The following is what I wished I’d known about them before I started studying them on my own.

First, mathematicians and physicists describe tensors so differently, that it’s hard to even see that they’re talking about the same thing (one math book of mine says exactly that). Also mathematicians basically dump on the physicists’ way of doing tensors.

My first experience with tensors was years ago when auditing a graduate abstract algebra course. The instructor prefaced his first lecture by saying that tensors were the hardest thing in mathematics. Unfortunately right at that time my father became ill and I had to leave the area.

I’ll write a bit more about the mathematical approach at the end.

The physicist’s way of looking at tensors actually is a philosophical position. It basically says that there is something out there, and how two people viewing that something from different perspectives are seeing the same thing, and how they numerically describe it, while important, is irrelevant to the thing itself (ding an sich if you want to get fancy). What a tensor tries to capture is how one view of the object can be transformed into another without losing the object in the process.

This is a bit more subtle than using different measuring scales (fahrenheit vs. centigrade). That salt shaker siting there looks a bit different to everyone present at the table. Relative to themselves they’d all use different numbers to describe its location, height and width. Depending on distance it would subtend different visual angles. But it’s out there and has but one height and no one around the table would disagree.

You’re tall and see it from above, while your child sees it at eye level. You measure the distances from your eye to its top and to its bottom, subtract them and get the height. So does you child. You get the same number.

The two of you have actually used two distinct vectors in two different coordinate systems. To transform your view into that of your child’s you have to transform your coordinate system (whose origin is your eye) to the child’s. The distance numbers to the shaker from the eye are the coordinates of the shaker in each system.

So the position of the bottom of the shaker actually has two parts (e.g. the vector describing it)
l. The coordinate system of the viewer
2. The distances measured by each (the components or the coefficients of the vector).

To shift from your view of the salt shaker to that of your child’s you must change both the coordinate system and the distances measured in each. This is what tensors are all about. So the vector from the top to the bottom of the salt shaker is what you want to keep constant. To do this the coordinate system and the components must change in opposite ways. This is where the terms covariant and contravariant and all the indices come in.

What is taken as the basic change is that of the coordinate system (the basis vectors if you know what they are). In the case of the vector to the salt shaker the components transform the opposite way (as they must to keep the height of the salt shaker the same). That’s why they are called contravariant.

The use of the term contravariant vector is terribly confusing, because every vector has two parts (the coefficients and the basis) which transform oppositely. There are mathematical objects whose components (coefficients) transform the same way as the original basis vectors — these are called covariant (the most familiar is the metric, a bilinear symmetric function which takes two vectors and produces a real number). Remember it’s the way the coefficients of the mathematical object transform which determines whether they are covariant or contravariant. To make things a bit easier to remember, contRavariant coefficients have their indices above the letter (R for roof), while covariant coefficients have their indices below the letter. The basis vectors (when written in) always have the opposite position of their indices.

Another trap — the usual notation for a vector skips the basis vectors entirely, so the most familial example (x, y, z) or (x^1, x^2, x^3) is really
x^1 * e_1 + x^2 * e_2 + x^3 * e-3. Where e_1 is (1,0,0), etc. etc.

So the crucial thing about tensors is the way they transform from one coordinate system to another.

There is a far more abstract way to define tensors, as the way multilinear products of vector spaces factor through it. I don’t think you need it for relativity (I hope not). If you want to see a very concrete to this admittedly abstract business — I recommend “Differential Geometry of Manifolds” by Stephen Lovett pp. 381 – 383.

An even more abstract definition of tensors (seen in the graduate math course) is to define them on modules, not vector spaces. Modules are just vector spaces whose scalars are rings, rather than fields like the real or the complex numbers. The difference, is that unlike fields the nonZero elements don’t have inverses.

I hope this is helpful to some of you

Newer isn’t better in web page display

Something bad has happened to the displays of the journals I read online (Nature, Science, Cell, Nature and PNAS). It’s also happened to this WordPress as it displays the blog. Suddenly it is no longer possible to expand what is shown horizontally. This is important (to me) as I’m slightly visually impaired, which requires enlarging text size for readability. Limiting horizontal expansion, while increasing text size means that there is less on each line. This makes reading more irritating than it needs to be.

For an example of where this still is not happening, see In the Pipeline by Derek Lowe.

Does anyone out there know of a workaround? I see the same problem in FireFox and Safari.

I’m going to write WordPress to see if they have any suggestions. Their help service is remarkable, friendly, fast and even more amazing — free

Could Alzheimer’s disease be a problem in physics rather than chemistry?

Two seemingly unrelated recent papers could turn our attention away from chemistry and toward physics as the basic problem in Alzheimer’s disease. God knows we could use better therapy for Alzheimer’s disease than we have now. Any new way of looking at Alzheimer’s, no matter how bizarre,should be welcome. The approaches via the aBeta peptide, and the enzymes producing it just haven’t worked, and they’ve really been tried — hard.

The first paper [ Proc. Natl. Acad. Sci. vol. 111 pp. 16124 – 16129 ’14 ] made surfaces with arbitrary degrees of roughness, using the microfabrication technology for making computer chips. We’re talking roughness that’s almost smooth — bumps ranging from 320 Angstroms to 800. Surfaces could be made quite regular (as in a diffraction grating) or irregular. Scanning electron microscopic pictures were given of the various degrees of roughness.

Then they plated cultured primitive neuronal cells (PC12 cells) on surfaces of varying degrees of roughness. The optimal roughness for PC12 to act more like neurons was an Rq of 320 Angstroms.. Interestingly, this degree of roughness is identical to that found on healthy astrocytes (assuming that culturing them or getting them out of the brain doesn’t radically change them). Hippocampal neurons in contact with astrocytes of this degree of roughness also began extending neurites. It’s important to note that the roughness was made with something neurons and astrocytes never see — silica colloids of varying sizes and shapes.

Now is when it gets interesting. The plaques of Alzheimer’s disease have surface roughness of around 800 Angstroms. Roughness of the artificial surface of this degree was toxic to hippocampal neurons (lower degrees of roughness were not). Normal brain has a roughness with a median at 340 Angstroms.

So in some way neurons and astrocytes can sense the amount of roughness in surfaces they are in contact with. How do they do this — chemically it comes down to Piezo1 ion channels, a story in themselves [ Science vol. 330 pp. 55 – 60 ’10 ] These are membrane proteins with between 24 and 36 transmembrane segments. Then they form tetramers with a huge molecular mass (1.2 megaDaltons) and 120 or more transmembrane segments. They are huge (2,100 – 4,700 amino acids). They can sense mechanical stress, and are used by endothelial cells to sense how fast blood is flowing (or not flowing) past them. Expression of these genes in mechanically insensitive cells makes them sensitive to mechanical stimuli.

The paper is somewhat ambiguous on whether expressing piezo1 is a function of neuronal health or sickness. The last paragraph appears to have it both ways.

So as we leave paper #1, we note that that neurons can sense the physical characteristics of their environment, even when it’s something as un-natural as a silica colloid. Inhibiting Piezo1 activity by a spider venom toxin (GsMTx4) destroys this ability. The right degree of roughness is healthy for neurons, the wrong degree kills them. Clearly the work should be repeated with other colloids of a different chemical composition.

The next paper [ Science vol. 342 pp. 301, 316 – 317, 373 – 377 ’13 ] Talks about the plumbing system of the brain, which is far more active than I’d ever imaged. The glymphatic system is a network of microscopic fluid filled channels. Cerebrospinal fluid (CSF) bathes the brain. It flows into the substance of the brain (the parenchyma) along arteries, and the fluid between the cellular elements (interstitial fluid) it exchanges with flows out of the brain along the draining veins.

This work was able to measure the amount of flow through the lymphatics by injected tracer into the CSF and/or the brain parenchyma. The important point about this is that during sleep these channels expand by 60%, and beta amyloid is cleared twice as quickly. Arousal of a sleeping mouse decreases the influx of tracer by 95%. So this amazing paper finally comes up with an explanation of why we spend 1/3 of our lives asleep — to flush toxins from the brain.

If you wish to read (a lot) more about this system — see an older post from when this paper first came out — http://luysii.wordpress.com/2013/10/21/is-sleep-deprivation-like-alzheimers-and-why-we-need-sleep-in-the-first-place/

So what is the implication of these two papers for Alzheimer’s disease?

    First

The surface roughness of the plaques (800 Angstroms roughness) may physically hurt neurons. The plaques are much larger or Alzheimer would never have seen them with the light microscopy at his disposal.

    Second

The size of the plaques themselves may gum up the brain’s plumbing system.

The tracer work should certainly be repeated with mouse models of Alzheimer’s, far removed from human pathology though they may be.

I find this extremely appealing because it gives us a new way of thinking about this terrible disorder. In addition it might explain why cognitive decline almost invariably accompanies aging, and why Alzheimer’s disease is a disorder of the elderly.

Next, assume this is true? What would be the therapy? Getting rid of the senile plaques in and of itself might be therapeutic. It is nearly impossible for me to imagine a way that this could be done without harming the surrounding brain.

Before we all get too excited it should be noted that the correlation between senile plaque burden and cognitive function is far from perfect. Some people have a lot of plaque (there are ways to detect them antemortem) and normal cognitive function. The work also leaves out the second pathologic change seen in Alzheimer’s disease, the neurofibrillary tangle which is intracellular, not extracellular. I suppose if it caused the parts of the cell containing them to swell, it too could gum up the plumbing.

As far as I can tell, putting the two papers together conceptually might even be original. Prasad Shastri, the author of the first paper, was very helpful discussing some points about his paper by Email, but had not heard of the second and is looking at it this weekend.

Coca-Cola

For some readers, this might be the most useful post I’ve ever written. But first; some history. Back in grad school, I was dating a Cliffie. We were out to dinner at a nice (and cheap) restaurant in Cambridge. I’d had the flu and probably should have canceled, but in your early 20s, libido conquers all. So we’re sitting there, and I began to feel really nauseous and said we should pack it in, and I should go home.

She said “Let me try this, my father’s a General Practitioner”. So she ordered a can of coke, opened it and let it sit for a while till it warmed up and the fizz was gone. Then she told me to drink it in slow, small sips. It worked ! The nausea vanished and we continued on.

Fast forward to last night and probable food poisoning (or severe flu). No Coke in the house, but as soon as my wife got to a store opening at 7 this AM, it worked again — no nausea and stomach distress within a few minutes (I’d vomited at least 5 times over the course of the night).

Could this have been a placebo effect, because it had worked in the past and I wanted it to work so desperately? Possibly, but I was generally miserable for a period for a period of 10 hours, and the Coke settled my stomach very quickly. Coke is not an anti-diarrheal, but 10 hours into the illness there was nothing left.

Placebos and Nocebos are very complicated entities and a huge review in Neuron will tell you why. It’s very much worth reading – Neuron vol 84 pp. 623 – 637 ’14 — “Placebo Effects: From the Neurobiological Paradigm to Translational Implications”. The article contains references to studies showing that placebo is as effective as morphine on the third day post-op. In med school I’d heard stories to the effect that in Korea and WWII when they ran out of morphine on the battlefield, saline worked just as well. So probably these aren’t myths. It didn’t happen in Vietnam when I was in the service, as the country is long and thin, and no wounded soldier was more than 20 minutes away by chopper from a fully equipped field hospital (once they got him).

The ingredients in Coke are and were a closely held secret, but most think in the 1880s and 1890s, when it was sold as a medication, that Coke contained cocaine, hence the name. Back then, no one knew the potential of cocaine for addiction. Halstead the great Baltimore surgeon, got into it because cocaine is also a local anesthetic. Freud actually used cocaine to treat morphine addiction. Neither was malevolent, just ignorant.

The peculiar blindness of the highly intelligent

This is not a scientific post. While at Graduate Alumni day last April at Harvard, I listened to the main speaker go on and on about how irrational (translation: stupid) people were when it came to risk, particularly that of flying after 9/11. In terms of miles traversed, flying is far safer than driving. The speaker was Louise Richardson
PhD ’89, government, presently Principal and Vice-Chancellor of the University of St Andrews. Her topic was “Terrorism: what have we learned?”

Here’s who she is and what she’s done. In the years after 9/11, in addition to her teaching and management roles, Professor Richardson gave over 300 talks and lectures on terrorism and counter-terrorism to educational and private groups as well as policy makers, the military, intelligence, and business communities. She has testified before the United States Senate and has appeared on CNN, NBC, the BBC, PBS, NPR, Fox and a host of other broadcast outlets. Her work has been featured in numerous international periodicals.

Clearly, she’s listened to. As I sat there I wondered how her advice for society could be any good, given her contempt for the way most of its members think. I’m sure in the several hundred of so listeners there were some adamantly opposed nuclear power. Two years previously we heard professor Daniel Schrag talk on a geologist’s perspective on global warming, saying there was no such thing as ‘clean coal’ and how slowly carbon dioxide is cleared from the atmosphere. Clearly, nuclear power is cleanest mode of energy production, with the lowest risk etc. etc. Why are some highly educated (and presumably intelligent) people against it?

Which brings us to the mind set of Professor Gruber. Amazingly, Howard Dean (a man of the left) had the following to say about Professor Gruber and Obamacare on MSNBC

First Gruber: “The problem is not that Gruber said it– the problem is that he thinks it”

Then ObamaCare “The core problem under the damn law is that it was put together by a bunch of elitists who don’t fundamentally understand the American people. That’s what the problem is”

How could free health care be so unpopular.

The common delusion of the highly intelligent is that since they think so well, everyone should think like them, and if they don’t their behavior and institutions should be directed by their intellectual betters. Nothing much has changed in Cambridge in 54 years. This mindset was just as common then as it is now. You can see how well it’s working.

Well, probably most readers of this blog are highly educated (technically at least), and years away from dealing with the mass of humanity. Most doctors in practice see the full spectrum of the populace, because everyone gets sick.

Here’s what’s out there. Part of the neurologic examination is the mental status examination. One assesses a variety of things — orientation, speech, affect, calculation, memory etc. etc. One part often used to assess higher cognitive function is the ability to abstract. People are asked things like, what’s similar about an apple and an orange, a table and a chair. What’s different about a river and a lake. They can be asked for the meaning of familial proverbs “a stitch in time saves nine, people who live in glass houses shouldn’t throw stones. The point of the mental status is to separate the normal from the abnormal.

I pretty much had to abandon similarities and differences because so many normally functioning people thought extremely concretely. For the apple/orange similarity I’d get back they’re both round, or (worse) one is red the other is orange (not a similarity), or the proverb would be repeated back verbatim. I’d guess that 1/3 of people think this concretely.That table and chair were both furniture or that apples and oranges were both fruit was only the response about 60% of the time. You can either call the 1/3 abnormal (which means you need to redefine normal) or decide that the test is useless for picking up pathology. I chose the latter.

This is why I’ll only interview high school students for my Ivy league alma mater (Princeton). Princeton needs them as much as they need Princeton. They bring a dose of reality to a very cloistered environment.

It’s why I don’t read novels

You can’t make up stuff like this. A nephrologist whom I consulted about our daughter-in-law’s bout with pre-eclampsia, asked me about her brother-in-law when she found out I’d been a neurologist. Long out of practice, I called someone in my call group still practicing, only to find out that his son (who was just a little guy when we practiced) is finishing up his PhD in Chemistry from Princeton. Put this in a novel and no one would believe it.

The reason for the post, is that Princeton’s new Chemistry building, built to the tune of .25 gigaDollars, isn’t working very well. According to his son not all the hoods are functional. There are other dysfunctionalities as well, lack of appropriate space etc. etc. All is not lost however, the building is so beautiful (if non-functional) that it is used as a movie set from time to time. Any comments from present or past inhabitants of the new building?

Here’s the old post.

Princeton Chemistry Department — the new Oberlin

When I got to grad school in the fall of ’60, most of the other grad students were from East and West coast schools (Princeton, Bryn Mawr, Smith, Barnard, Wheaton, Cal Tech etc. etc.), but there were two guys from Oberlin (Dave Sigman, Rolf Sternglanz) which seemed strange until I looked into it. Oberlin, of course, is a great school for music but neither of them was a musician. They told me of Charles Martin Hall, Oberlin alum and inventor of the Hall process for Aluminum — still used today. He profited greatly from his invention, founding what is today Alcoa, running and owning a lot of it. He gave tons of money to the Oberlin Chemistry department, which is why it was so good back than (and probably still is).

What does this have to do with Princeton? Princeton’s Charles Hall is emeritus prof Ted Taylor, whose royalties on Alimta (Pemetrexed), an interesting molecule with what looks like guanine, glutamic acid, benzoic acid and ethane all nicely stitched together to form an antifolate, to the tune of over 1/4 of a billion dollars built the new Princeton Chemistry building. Praise be, the money didn’t go into any of the current academic fads (you know what they are), but good old chemistry.

An article in the 11 May “Princeton Alumni Weekly” (yes weekly) about the new building contains several other interesting assertions. The old chemistry building is blamed for a number of sins e.g., “no longer conducive to the pursuit of cutting-edge science in the 21st century”, “hard to recruit world-class faculty and grad students to what was essentially rabbit warren” etc. etc. Funny, but we thought the place was pretty good back then.

When the University president (Shirley Tilghman, a world-class molecular biologist prior to assuming the presidency — just Google imprinting) describes Princeton Chemistry as ‘one of Princeton’s “least-strong departments” you know there are problems. Is this really true? Maybe the readership knows.

Grad school applications are now coming from the ‘very top applicants’ — is it that easy to rate them? This is said not to be true 10 years ago — wonder how those now with PhD’s entering the department back then feel about this.

Then there is a picture of a young faculty member “Abby Doyle” who joined the department 6 years after graduating Harvard in 2002. As I recall there was a lot of comment on this in the earlier incarnation of ChemBark a few years ago.

The new building is supposed to inspire collaboration because of its open space, and 75 foot atrium, ‘few walls between the labs and glass is everywhere’. Probably the article was written by an architect. The implication being is that all you need for good science is a good building, and that bad buildings can inhibit good science. Anyone out there whose science has blossomed once they were put in a glass cage?

It’s interesting to note that the undergraduate catalog for ’57 – ’58 has Dr. Taylor basically in academic slobbovia — he’s only teaching Chem 304a, a one semester course “Elementary Organic Chemistry for Basic Engineers” (not even advanced engineers)

Comments anyone?

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