Studies of the Aromatic Circular Dichroism of Staphylococcal Nuclease

Studies of the Aromatic Circular Dichroism of Staphylococcal Nuclease

Contributor(s):
Anfinsen, Christian B. (Christian Boehmer), 1916-1995
Proceedings of the National Academy of Sciences of the United States of America
Omenn, Gilbert S.
Cuatrecasas, Pedro
Publication:
National Academy Press (U.S.), November 1969
Language(s):
English
Format:
Text
Subject(s):
Binding Sites
Circular Dichroism
Deoxyribonucleases
Ribonucleases
Genre(s):
Archival Materials
Articles
Abstract:
In this article, Anfinsen, Omenn, and Cuatrecasas described the circular dichroism spectra of nuclease and of performic acid-oxidized derivative. Their findings suggested that the binding of the nucleotide inhibitor altered the asymmetric environment of certain tyrosyl residues. Furthermore, through titration, a method which can determine a substance or component in a solution by the addition of a liquid reagent of a known strength until a given endpoint, they were subsequently able to determine with greater certainty several of the amino acids present in the amino chain for staphylococcal nuclease.
Copyright:
This item may be under copyright protection; contact the copyright owner for permission before re-use.
Extent:
8 pages
NLM Unique ID:
101584571X174 (See in Profiles in Science)
Profiles in Science ID:
KKBBLJ
Permanent Link:
http://resource.nlm.nih.gov/101584571X174
Archival Collection:
The Christian B. Anfinsen Papers (Profiles in Science)