- 22.70 Bill of sale [?] in German [Filed under LP Safe: Box 3.022, Folder 22.70]
- Deposit slip for LP's account at Southern Commercial and Savings Bank: Total amount deposited $12,000 (Nobel Prize Award) [LP Biographical: Box 4.023, Folder 23.3]
- Letter from K.H. Gustavson to LP. [Filed under LP Science: (Materials re: The Structure and Properties of Collagen, 1951-1955), Box #6.004, Folder #4.16]
Dear Dr. Pauling:
As an old-timer of the Collagentsia-quite solo in these parts- I am inconsiderate enough to detract the strained Nobel-laureate from the extraverts of the day to the intraverts of collagen. A few lines reading on some recent developments in the chemistry of collagen might then be a relaxation.
According to the findings given in the enclosed notes, the degree of the hydrothermal stability of collagens is directly related to their content of hypro (from 70° to 35° versus hypro % from 13 to 6). Investigations of exhaustively acetylated bovine collagens indicate 3 out of 4 hypro-OH groups to form the link - OH ••••• OC. The OH group resisting acetyla-tion appears to be the mainstay of collagens structure HN, generally. By O-acetylation of bovine collagen, i.e., the breaking of the hydrogen bonds given above, its shrinkage temperature is lowered from 65 to 40°, or to the point of teleostian collagen. There are some indications that the link responsible for the ultimate stability of collagen is an ester link of the type -0 • CO. Thus, Grassmann (the Aug. issue of Z. Naturforschung) cites exp. evidence suggesting the presence of an ester link in procollagen. Collagen is insoluble in sat. solution of LiBr, whereas silkfibroin and synthetic polypeptides, mainly H-bonded, are easily solubilized. The alkoli binding capacity of limed collagens is about 0.5 meq. base per g. collagen, while gelatin binds 0.8 - 0«,9 meq. The free caxboxyl groups amount to about 1 meq. per g. protein in both instances. The presence of the masked OH groups (0.3 – 0.4 meq.) in ester linking with carboxyl groups would satisfactorily account for the difference.
As to the interchain nature of the OH •••• CO link, deduced from the trend of the TS, this canlusion would be invalidated if an intrachain link of this type would suffice for the hydrothermal stabilization of collagen. Thus, according to Huggins model in his recent JACS-note, an intrachain hydrogen bond of the type suggested by me is assigned a distance of 2.9 Å. If you might get a chance looking into this, it would be fine to have a chat with you at the social tea after your Tuesday-night lecture. No writing or acknowledging please.
Finally, a recent finding of Zahn published in a leather chemist journal, which likely is not available in Pasadena, will undoubtedly interest you. By making a sulfone out of Sanger's reagent, an excellent crosslinking agent for collagen is obtained. By hydrolysis of the sulfone-treated collagen and the dinitrodiphenylsulfone-bis-lysine was isolated. I am enclosing a reprint, by the way. Evidently, the two lysine residues are close enough to be within the reach of the S-connected benzene rings. The may be conceived as supporting Bear's idea of the bulky side chains being located in the bands and the matching of the bands in fibrils. In my Cincinnati lecture, as you perhaps remember, I stressed the fact that by crosslinking of collagen its hydrothermal stability is improved, while the cross-linking has practically no effect of the mechanical strength of the fibers (cohesion), explaining some findings of our mutual friend John Highberger. This issue takes on a new aspect if the hydrothermal stabilization should be due to intrahelical crosslinking.
These simple demonstrations may be of helpful in attempts of promulgating structures for collagen. Your helical concept has stirrd the thinking members of my scribe. We thank you for your impulses and your inspiration and we wish you health and solitude for the final arrival.
With kind personal regards,
- Letter from Naturvetenskapliga Foreningen Vid Stockholms Hogskola, December 13, 1954. [Filed under LP Biographical: Box 6.006, Folder 6.87]
- Lucia-entertainment at 7:30, given by the Students' Association for Natural Science at the University of Stockholm.
- Magazine Article: “Franklin’s Heirs Meet, Speak and Ponder,” Life Magazine, December 13, 1954. [Filed under LP Science: (American Philosophical Society, 1936-1963, 1989, 1991), Box #14.011, Folder 11.2]
- Newspaper Clipping: "Julklappskop och Lucia for Nobelpristagarna", Dagens Nyheter, December 13, 1954. [Filed under LP Biographical: Box 6.006, Folder 6.89]
- Newspaper Clipping: "Party for Nobelpristagare", Svenska Dagbladet [Filed under LP Biographical: Box 6.006, Folder 6.121]
- Newspaper Clipping: "Party fr Nobelpristagare",Svenska Dagbladet (Stockholm), December 13, 1954. [LP Newspaper Clippings 1954n2.32]
- Newspaper Clipping: "The Polar Route to Deserved Acclaim", Publication Unknown, December 13, 1954. [LP Newspaper Clippings 1954n2.31]
- Note from Carl Dyster, The Mirror to LP RE: Enclosed tearsheets of interview with LP, published December 9, 1954 [Reply Beatrice Wulf December 16, 1954] [Filed under D: Correspondence 1954, Box #98.19]
- Photo: Linus Pauling receiving the Award of the Order of the Ever-Jumping Green Frog. An unidentified man wearing a black robe and cowl standing and holding a sign decorated by crude illustrations and runes. University of Stockholm, Sweden. "Award of the 'Order of the Ever-Jumping Green Frog' to Linus Pauling. -Lucia Dag, University of Stockholm Dec. 13, 1954 / Photo by Olle Bjönkman" Black and white print. December 13, 1954. [Filed under LP Photographs: 1954i.47]
- Photo: Linus Pauling wearing a tuxedo for the 1954 Lucia Celebration at the University of Stockholm. Stockholm, Sweden. "Lucia Celebration, National Science Association of the University of Stockholm December 13, 1954 / Photo by Olle Bjönkman" Black and white print. December 13, 1954. [Filed under LP Photographs: 1954i.46]
- Program for Luciadagen (St. Lucia Day Festival); sketch in the corner of St. Lucia [1954 Nobel Prize in Chemistry Notebook]
- Reception at the American Embassy, given by Mrs. Cabot, between 5 and 7 p.m.