Asparagine and glutamine differ in their propensities to form specific side chain-backbone hydrogen bonded motifs in proteins

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 4, 2012, Pages 991-1002

  Vasudev, Prema G ^a   Banerjee, Mousumi ^a   Ramakrishnan, C ^a   Balaram, P ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Asparagine residue; Glutamine residue; Neutral polar residues; Protein structures; Side chain backbone hydrogen bonds

Indexed keywords

ASPARAGINE; GLUTAMINE;

ALPHA CHAIN; ARTICLE; ATOM; BETA CHAIN; CRYSTAL STRUCTURE; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; ASPARAGINE; COMPUTATIONAL BIOLOGY; GLUTAMINE; HISTIDINE; HYDROGEN BONDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 84857728201     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24001     Document Type: Article

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