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W r i n c h Discusses Proteins in Stieglitz Lecture A STAFF R E P O R T
A HKORIES of p r o t e i n s t r u c t u r e were dis cussed b y D o r o t h y Wrinch, of Smith College, a s t h e Stieglitz Memorial Lec turer J a n . 24. T h e lecture was held in P a t t o n G y m n a s i u m , Northwestern Uni versity, K v a n s t o n , 111., as t h e conclusion of t h e second all-day Technical Confer ence of t h e Chicago Section of t h e A M E R I CAN C H E M I C A L SOCIETY.
II. K. Summer-
bell, of N o r t h w e s t e r n University and chairman of t h e Chicago Section, presided a t t h e meeting, and Β . Β. F r e u d , of Illinois I n s t i t u t e of Tech nology, introduced the lecturer. Dr. F r e u d w a s a close friend of Stieglitz and served as treas urer in establishing t h e Stieglitz lec tureship fund. Nearly 500 at tended t h e lecture. Announcing as Β. Β. Freud her premise t h a t protein is an entity, D r . Wrinch reviewed evidence to s u p p o r t this view and concluded t h a t recent work in physical chemistry a n d chemical crystal lography yields a definite a n d precise picture of t h e s t r u c t u r e of n a t i v e protein. T h e i n s t a b i l i t y of t h e protein molecule, or p r o t e o n , a p p a r e n t l y resides in t h e skele ton, asserted D r . W r i n c h . E a c h proteon m a i n t a i n s its existence only in virtue of the associations of favorably juxtaposed R - s u b s t i t u e n t s . T h i s precarious stability m a y be intramolecular o r it m a y depend also on some intermolecular R-group as sociations. T h e proteon skeleton, t h o u g h unstable, is rigid. In t h i s w a y associations of Rgroups which, are configurationally defi nite are m a d e possible. T h e p r o t e i n character resides in t h e ex tremely well-defined, though a t present u n k n o w n , s t r u c t u r e of proteon skeletons. "This, w e expect, will prove t o be as defi nite an e n t i t y a s t h e carbon skeleton of t h e sterols o r t h e carbon-nitrogen skeleton of h e x a m e t h y l e n e t e t r a m i n e . Alternatively it m a y t u r n o u t to b e a homologous series of e n t i t i e s , each of this degree of denniteness, e m b o d y i n g some common construc tional principle." T h e particular composition of a n indi vidual p r o t e o n resides i n t h e particular numbers of individual R-groups (alanines, arginines, etc.) among its substituents. T h e fact t h a t definite configurations of R-group associations are t h e common fac tor in f u n d a m e n t a l phenomena of enzyV O L U M E
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mology, immunology, pharmacology, and other fields of protein studies makes it a p p e a r likely t h a t this same factor m a y throw light on t h e n a t u r e of biosynthesis of protein molecules. The
Lecturer
Dorothy Wrinch, mathematician, chem ist, a n d biologist, was born in Argentina and educated in England and o n the Con t i n e n t . She holds degrees from C a m bridge, London University, a n d Oxford where she was a member of t h e faculty of physical sciences for m a n y years. In 1935, Dr. Wrinch came t o the United States at t h e invitation of the Rockefeller Foundation which until 1941 sponsored her new studies in t h e application of m a t h e matics to structure problems of biology and medicine. In 1939 she became lec turer in chemistry a t J o h n s Hopkins Uni versity, leaving in 1941 t o become visiting professor a t Amherst, M t . Holyoke, and Smith Colleges. Since 1942 s h e has been lecturing in t h e physics department of Smith College with her s u m m e r activities centered n t t h e Woods Hole M a r i n e Bio-
Darothy
Wrinch
logical Laboratory. In 1943 she became a n American citizen. Dr. Wrinch is t h e wife of O. C. Glaser, professor of biology at Amherst College. Her daughter is a junior a t t h e University of Michigan. Dr. Wrinch/s work has covered a wide field, mainly pure mathematics, mathe matical physics, a n d probability theory. Since 1934 she has been mainly concerned with theoretical chemistry, particularly n a t i v e proteins, a n d molecular biology; most recently, crystallography.
The Stieglitz Lecture A HE STIEGLITZ lectureship, founded in 1940 by t h e Chicago Section of t h e AMERICAN CHEMICAL SOCIETY a n d t h e
alumni of t h e chemistry d e p a r t m e n t of t h e University of Chicago, honors t h e memory of Jul ius Stieglitz, distinguished chemist and professor, and symbolizes t h e b r e a d t h of his interest in sci ence a n d t h e arts. T h e lec t u r e r is chosen b y the university to speak in a field of chemistry related t o those in which Stieglitz worked. T h e lecture is alter nated annually between t h e Chicago Section and the university. Stieglitz' work in organic chemistry embraced several interrelated fields a n d is described in 6 6 research papers a n d t h e theses of U S doctors who took their degrees with h i m . I n addition, Stieglitz will long b e remembered for h i s contributions to analytical chemis
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try a n d for h i s lucid and meticulous lectures. Stieglitz was born in Hoboken, N. J . , in 1867. His boyhood a n d elementary schooling were passed in N e w York City, and a t t h e age of 14 his family took h i m and his brothers t o Germany t o complete their education. Returning t o this country in 1890, Stieglitz worked for two years as a toxicologist with P a r k e , Davis a n d Co. b u t went t o t h e University of Chicago a s docent under Kef in 1S92. H e rose t o professor in 1905, chairman of t h e chemistry d e p a r t m e n t in 1915. An exponent of chemotherapeutic research, Stieglitz' lifelong interest in medicine found expression in his vice chairmanship of t h e Council of Phar macy and Chemistry of t h e American Medical Association, 1905-24, and his editorship of " C h e m i s t r y in Medicine", published by t h e Chemical Foundation. Recipient of m a n y honors, Stieglitz was president of t h e AMERICAN CHEMICAL
SOCIETY i n 1917.
Retiring in 1933,
Steiglitz continued his work as emeritus professor u n t i l his death, J a n . 10, 1937.
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