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Correspondence
| LP to Jerry Donohue. January 20, 1953. |
LP to Jerry Donohue - Page 01
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Authors: Linus Pauling, Jerry Donohue
LP to Jerry Donohue - Page 01
| Title: |
Linus Pauling's reply to Jerry Donohue [1 of 2] |
| Alternative Title: |
Linus Pauling's reply to Jerry Donohue, Jan. 20, 1953 |
| Creator: |
Pauling, Linus, 1901- |
| Publisher: |
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| Date: |
1953-01-20 |
| Subject: |
Chemical structure
Pauling, Linus, 1901- -- Correspondence
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| Description: |
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| Type: |
Text |
| Format: |
text/plain |
| Language: |
en |
| Identifier: |
donohue04-pg08 |
| Source: |
Master file format: TIFF, 600 dpi, Epson GT-10000+ flatbed scanner. |
| Rights: |
http://osulibrary.oregonstate.edu/specialcollections/coll/pauling/dna/copyright.html |
| Full Text: |
Dear Jerry: the heart is in various activities have keep me from answering your letter of 16 December until now. I asked Yakel
to check over the calculations of the radial distribution functions for the alpha helix, and he has done so. He has reported
to be at the interatomic distances that were used seem to agree with those that he is calculated, to within about 0.1 A. accordance
that were used in the calculations are, in fact, not those given an unpublished table (which refers to a 3.6-residue helix),
but those obtained about a year earlier. They correspond to a 3.67-residue helix -- the helix with 11 residues in three turns.
I think that this movie functions that we used is one that I devised on the basis of information that he gave me. It involves
spending each point out over about 0.5 A to either side. I think that it does in between yours for B=2 and B=4. I send details
about our smoothing function to Riley, and it is likely that it does not differ much from the one that he used. It is not
clear to me whether the difference between our calculated curves and yours (and Riley's) is due to a difference in coorinates,
or to something else. Perhaps we missed the double peak at 5 A for beta carbon 2 because of an erorr in one of our points.
Yakel, Schatz, and Rack have completed them work on cylindrical distribution function. They have evaluated the cylindrical
distribution functions for alpha keratin and also for collagen from the experimental fiber diagrams, and they have evaluated
the cylindrical distribution function for the alpha helix, using accordance for the 3.67-residue helix as the starting point.
There is only by agreement between the theoretical function in the experimental function for alpha keratin. There is, of
course, disagreement for collagen. I expect you have seen our article in nature, on the alpha keratin proteins. We have
made more detailed calculations, they have not yet when the material up for publication and that proceedings. That's how
you that Corey and I have said the paper on the structure of the plate acids off to the proceedings for publication? It will
appear in the February issue. As to Carlisle, I went over his material on ribonuclease with him and Bernal this summer.
I reach the conclusion that Founier diagrams that he obtains, and adduces as evidence against alpha helix is in favor of a
ribbin structure, popular artifacts-that there is no justification for assuming the signs of Fourier turns into a day he dies.
There is, of course, the possibility that
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