학술논문
Heat and cold denatured states of monomeric lambda repressor are thermodynamically and conformationally equivalent
Document Type
Academic Journal
Author
Source
Biochemistry. May 21, 1996, Vol. 35 Issue 20, p6173, 8 p. table
Subject
Language
ISSN
0006-2960
Abstract
The structures of the heat and cold denatured states of monomeric bacteriophage lambda repressor are thermodynamically and conformationally the same. The aromatic 1H nuclear magnetic resonance (NMR) spectra of the urea denatured and thermally denatured states are the same at 37 degrees Celsius. The circular dichroism and NMR studies of thermal and urea denaturation of residues 6-85 of the N-terminal region of lambda repressor indicate that the totally denatured state is the sole non-native state at temperatures over 25 degrees Celsius.