α-helix stabilization by alanine relative to glycine: Roles of polar and apolar solvent exposures and of backbone entropy

Proteins: Structure, Function and Genetics

Volumn 64, Issue 3, 2006, Pages 769-778

  Lopez Llano J ^a   Campos, L A ^a   Sancho, J ^a   Sancho, Javier ^a  

^a UNIVERSITY OF ZARAGOZA   (Spain)

Author keywords

helix energetics; Backbone entropy; Protein folding; Protein stability; Solvent exposure

Indexed keywords

ALANINE; APOFLAVODOXIN; FLAVOPROTEIN; GLYCINE; SOLVENT; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ARTICLE; ENERGY TRANSFER; ENTROPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; SOLVENT EFFECT;

ALANINE; APOPROTEINS; CIRCULAR DICHROISM; COMPUTER SIMULATION; ENTROPY; FLAVODOXIN; GLYCINE; HYDROGEN BONDING; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SOLVENTS; THERMODYNAMICS;

EID: 33746267369     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21041     Document Type: Article

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