Satisfaction of hydrogen-bonding potential influences the conservation of polar sidechains

Proteins: Structure, Function and Bioinformatics

Volumn 75, Issue 2, 2009, Pages 413-429

  Worth, Catherine L ^a,b   Blundell, Tom L ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

Author keywords

Buried residues; Hydrogen bonds; Polar sidechains; Protein stability; Protein structure

Indexed keywords

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; HYDROGEN BOND; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STABILITY; PROTEIN STRUCTURE; CHEMISTRY; ENTROPY; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

AMINO ACID; PROTEIN;

AMINO ACID SEQUENCE; AMINO ACIDS; CONSERVED SEQUENCE; ENTROPY; HYDROGEN BONDING; HYDROPHOBICITY; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 66149139802     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22248     Document Type: Article

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