The sequence TGAAKAVALVL from glyceraldehyde-3-phosphate dehydrogenase displays structural ambivalence and interconverts between α-helical and β-hairpin conformations mediated by collapsed conformational states

Journal of Peptide Science

Volumn 13, Issue 5, 2007, Pages 314-326

  Patel, Sunita ^a   Balaji, Petety V ^a   Sasidhar, Yellamraju U ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Bend; GROMACS; Helix to hairpin transition; Molecular dynamics; Peptide model; Protein folding; Structural ambivalence; Turn

Indexed keywords

ALANINE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCINE; LYSINE; THREONINE; VALINE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENERGY; ENZYME STRUCTURE; GEOBACILLUS STEAROTHERMOPHILUS; HYDROPHOBICITY; MOLECULAR DYNAMICS; NONHUMAN; NORMAL DISTRIBUTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION;

BACILLUS STEAROTHERMOPHILUS; BACTERIAL PROTEINS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; MODELS, MOLECULAR; OLIGOPEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 34248355596     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.843     Document Type: Article

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