Conformational changes accompanying the binding of antithrombin III to thrombin
- 6 March 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (5) , 810-817
- https://doi.org/10.1021/bi00572a011
Abstract
The conformational aspects of the binding of [human] antithrombin III to thrombin were investigated by difference spectroscopy, circular dichroism [CD] and optical rotatory dispersion [ORD]. The CD and ORD studies indicated an increase of 6-8% in .alpha.-helix content at the expense of the .beta.-structure, while the results from difference spectroscopy showed an increased exposure of approximately 7 tyrosine residues. With heparin there was a slightly greater increase in helicity which was accompanied by exposure of an average of 1 tyrosine and 2 tryptophan residues. These spectral results indicated that the thrombin-antithrombin III complex formed with heparin differs in its conformation from that produced without it.This publication has 17 references indexed in Scilit:
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