PMID: 7013843Dec 1, 1980Paper

Hydrogen exchange in hydrated films of proteins. Application to the E. coli lac repressor core

Biophysical Chemistry
J PiletJ C Maurizot

Abstract

An original easy method of hydrogen to deuterium exchange in hydrated films of proteins, followed by infrared absorption measurements, is described and applied to films of the E. coli lac repressor core, in order to examine the effect of isopropyl-beta-D-thiogalactoside (IPTG) binding. An estimation of about 25% alpha helical structure in this protein fragment is deduced from the exchange curve. The binding of IPTG to the core does not affect the exchange curve within the experimental error limits.

References

Jun 15, 1976·Biochimica Et Biophysica Acta·M Nakanishi, M Tsuboi
May 14, 1979·Biochemical and Biophysical Research Communications·J RamsteinC Hélène
Oct 1, 1979·Biopolymers·S BourgeoisT T Wu
Jul 25, 1975·Journal of Molecular Biology·P Y ChouG D Fasman
Jan 15, 1974·Biochemistry·P Y Chou, G D Fasman
Jan 1, 1972·Annual Review of Biochemistry·S W EnglanderH Teitelbaum
Oct 28, 1969·Journal of Molecular Biology·S W Englander, R Staley
Mar 31, 1970·Biochemistry·S L Laiken, M P Printz
Mar 30, 1990·Science·K A Ream

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Citations

Oct 29, 1982·Molecular and Cellular Biochemistry·C WoodwardE Tüchsen

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