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The Joshua Lederberg Papers

Title:
Letter from Christian B. Anfinsen to Joshua Lederberg Annotation pdf (59,443 Bytes) ocr (1,528 Bytes)
Letter from Christian B. Anfinsen to Joshua Lederberg
Number of Image Pages:
1 (59,443 Bytes)
Date:
1956-08-20 (August 20, 1956)
Creator:
Anfinsen, Christian B.
Recipient:
Lederberg, Joshua
Rights:
Reproduced with permission of Libby Anfinsen.
Relation:
Lederberg Grouping: Correspondence C
Box Number: 8
Folder Number: 170
Unique Identifier:
BBACCZ
Accession Number:
5
Document Type:
Letters (correspondence)
Language:
English
Format:
application/pdf
image/tif
Physical Condition:
Good
Series: Correspondence, 1935-2002
SubSeries: 1953-1960
Folder: Anfinsen, Christian B.
Metadata Last Modified Date:
2005-06-14
Linked Data:
RDF/XML     JSON     JSON-LD     N3/Turtle     N-Triples

Annotation by Joshua Lederberg:
Node: Anfinsen, Christian.  Nobel Prize 1972; died 5/95;
cf obituary statement at Pontifical Academy of sciences;
I got to know him well as a clounselor to the Weizmann Institute
of Science, Rehovoth, Israel; and always found him wise and generous.
His experiment on the reconstitution of lysozyme activity after denaturation,
compounded with the demonstration of enzymatic activity of synthetic
lysozyme was a cornerstone of seuquence-determinism of protein biological
activity.



KW:P-56; genetic transduction; Calvin (eobiology);


"I have just finished reading your interesting article in the American Scientist
and want to thank you for the pleasant hour or so I spent with it. ..
reprints having to do with the general area of transduction, ...
do a fast job of reeducation ( and education for that matter, never having had
any formal biological training) in the areas of genetics, paleontology,
general biology
and the like since even a mild exposure to the study of the structure of proteins
and to the fascinating variations that occur from species to species and thru
the phyla makes one realize that the time has come for the protein chemist to
start to think in terms of genetics at the covalent bond level. The lessons to be
learned from a study of the evolutionary trends in the structure of specific
proteins will certainly be immensely valuable and I can't help feeling that
such studies will impose restrictions on the protein biosynthetic mechanisms
that will be of help in working out patternization procedures."


jl 12/23/98