Stabilization of the ribonuclease S‐peptide α‐helix by trifluoroethanol

Proteins: Structure, Function, and Bioinformatics

Volumn 1, Issue 3, 1986, Pages 211-217

  Nelson, Jeffrey W ^a,b   Kallenbach, Neville R ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b LOUISIANA STATE UNIVERSITY   (United States)

Author keywords

circular dichroism; peptide structural stability; protein electrostatics; protein folding; helix stabilization

Indexed keywords

PEPTIDE FRAGMENT; RIBONUCLEASE; RIBONUCLEASE S-PEPTIDE; S PEPTIDE; TRIFLUOROETHANOL;

ARTICLE; CIRCULAR DICHROISM; DRUG EFFECT; PH; PROTEIN CONFORMATION;

CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RIBONUCLEASES; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; TRIFLUOROETHANOL;

EID: 0022804939     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.340010303     Document Type: Article

References (18)

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