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Internal motion at the chloride binding sites of human serum albumin by NMR relaxation studies
Author(s) -
Bull Thomas E.,
Halle Bertil,
Lindman Björn
Publication year - 1978
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(78)80090-8
Subject(s) - center (category theory) , chemistry , chemical shift , relaxation (psychology) , library science , polymer science , medicine , computer science , crystallography
1. Introduction Evidence is rapidly growing for the presence of very fast internal motion in biological macromolecules [l- 51 and it seems reasonable to believe that the internal mobility is often involved in the functional role of the macromolecule. A rich variety of rapid motional phenomena in proteins is also a result of recent theoretical studies [6] and these authors stress the importance to have available methods which may in detail test the dynamic situation. There is, however, a pronounced lack of physico-chemical techniques which allow us to monitor these internal motion processes and, in particular, of methods which allow us to specifically study those internal motions which may be related to the biological function of the system, for example processes occurring at the active site of an enzyme. The purpose of this communication is to describe attempts to use 35C1 NMR relaxation investigations for studying internal mobility phenom- ena at the anion binding sites ofhuman serum albumin. Although a detailed quantitative interpretation of results of this type is quite difficult we will be able