Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C′ position of the C-capping box of α-helices

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

Volumn 98, Issue 19, 2001, Pages 10670-10675

  Thomas, Susan T ^a,b   Loladze, Vakhtang V ^a   Makhatadze, George I ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF TEXAS AT SAN ANTONIO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMIDE; AMINO ACID; ARGININE; ASPARAGINE; ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINE; GLYCINE; HISTIDINE; HYDROGEN; ISOLEUCINE; LYSINE; METHIONINE; PEPTIDE; PHENYLALANINE; PROLINE; SERINE; THREONINE; TRYPTOPHAN; UBIQUITIN; VALINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CORRELATION FUNCTION; ENTHALPY; ENTROPY; HYDRATION; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; QUANTUM CHEMISTRY; STATISTICAL ANALYSIS;

AMINO ACID SUBSTITUTION; DATA INTERPRETATION, STATISTICAL; PEPTIDES; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; UBIQUITINS; VALINE; WATER;

EID: 0035845493     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.191381798     Document Type: Article

References (40)