The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: Tools for protein design

Protein Engineering, Design and Selection

Volumn 29, Issue 7, 2016, Pages 271-280

  Childers, Matthew Carter ^a   Towse, Clare Louise ^a   Daggett, Valerie ^a  

^a University of Washington   (United States)

Author keywords

chirality; conformational propensity; denatured state; host guest series; intrinsic propensity; molecular dynamics simulation

Indexed keywords

CHAINS; CHIRALITY; DIHEDRAL ANGLE; METALS; MOLECULAR DYNAMICS; PROTEINS; UREA;

CONFORMATIONAL PROPENSITY; DENATURED STATE; HOST-GUESTS; INTRINSIC PROPENSITY; MOLECULAR DYNAMICS SIMULATIONS;

AMINO ACIDS;

ALANINE; GLUTAMIC ACID; HISTIDINE; PENTAPEPTIDE; UREA; WATER; OLIGOPEPTIDE; PROTEIN;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CHIRALITY; COMPARATIVE STUDY; CONTROLLED STUDY; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; STEREOSPECIFICITY; AMINO ACID SEQUENCE; CHEMISTRY; MOLECULAR DYNAMICS; PROTEIN DENATURATION; STEREOISOMERISM;

ALANINE; AMINO ACID SEQUENCE; MOLECULAR DYNAMICS SIMULATION; OLIGOPEPTIDES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; STEREOISOMERISM;

EID: 84977118900     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzw023     Document Type: Article

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