Urea unfolding of peptide helices as a model for interpreting protein unfolding

Proceedings of the National Academy of Sciences of the United States of America

Volumn 92, Issue 1, 1995, Pages 185-189

  Scholtz, J Martin ^a,b   Barrick, Doug ^a,d   York, Eunice J ^c   Stewart, John M ^c   Baldwin, Robert L ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b TEXAS A AND M UNIVERSITY   (United States)

^c UNIVERSITY OF COLORADO   (United States)

^d UNIVERSITY OF OREGON   (United States)

Author keywords

denaturant effects; helix coil transition; model peptide helix

Indexed keywords

UREA;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CIRCULAR DICHROISM; MODEL; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS;

AMINO ACID SEQUENCE; ANIMAL; CIRCULAR DICHROISM; COMPARATIVE STUDY; ENZYMES; MATHEMATICS; MODELS, THEORETICAL; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; THERMODYNAMICS; UREA;

EID: 0028950079     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.92.1.185     Document Type: Article

References (52)