Accessible surfaces of beta proteins increase with increasing protein molecular mass more rapidly than those of other proteins

PLoS ONE

Volumn 6, Issue 12, 2011, Pages

  Glyakina, Anna V ^a,b   Bogatyreva, Natalya S ^a   Galzitskaya, Oxana V ^a  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^b INSTITUTE OF MATHEMATICAL PROBLEMS OF BIOLOGY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARAGINE; ASPARTIC ACID; GLOBULAR PROTEIN; GLYCINE; SERINE; THREONINE; PROTEIN;

ACCESIBLE SURFACE AREA; ALPHA CHAIN; ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA CHAIN; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROGEN BOND; MOLECULAR WEIGHT; PROTEIN ANALYSIS; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE; PROTEIN VARIANT; STRUCTURE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; PROTEIN SECONDARY STRUCTURE;

AMINO ACIDS; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 82455206265     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0028464     Document Type: Article

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