Molecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin

Biochemistry

Volumn 54, Issue 2, 2015, Pages 505-515

  Banerjee, Priya R ^a   Pande, Ajay ^a   Shekhtman, Alexander ^a   Pande, Jayanti ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INTERFACE STATES; MAGNETIC DOMAINS; MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

C-TERMINAL DOMAINS; C-TERMINAL EXTENSIONS; CHAPERONE FUNCTIONS; MOLECULAR MECHANISM; REVERSIBLE BINDING; SMALL HEAT SHOCK PROTEINS; STRUCTURAL FEATURE; SUBSTRATE PROTEINS;

PROTEINS;

ALPHA CRYSTALLIN; CHAPERONE; GAMMA CRYSTALLIN; HUMAN GAMMA DEXTRO CRYSTALLIN; MINI ALPHA CRYSTALLIN; UNCLASSIFIED DRUG; CRYGD PROTEIN, HUMAN; PEPTIDE FRAGMENT; PROTEIN AGGREGATE; PROTEIN BINDING;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN UNFOLDING; TEMPERATURE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN STABILITY;

ALPHA-CRYSTALLIN A CHAIN; AMINO ACID SEQUENCE; GAMMA-CRYSTALLINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN AGGREGATES; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN UNFOLDING;

EID: 84922469706     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5014479     Document Type: Article

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