Helix formation and the unfolded state of a 52-residue helical protein

Protein Science

Volumn 13, Issue 1, 2004, Pages 177-189

  Cao, Wei ^a   Bracken, Clay ^a   Kallenbach, Neville R ^b   Lu, Min ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

^b NEW YORK UNIVERSITY   (United States)

Author keywords

Helix formation; NMR; Protein folding; Protein structure; Unstructured proteins

Indexed keywords

ALANINE; AMINO ACID; ASPARTIC ACID; GLUTAMINE; LYSINE; PROLINE; PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

ALANINE; AMINO ACID SEQUENCE; AMINO ACIDS; CIRCULAR DICHROISM; DIMERIZATION; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOTION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; RECOMBINANT PROTEINS; TEMPERATURE; ULTRACENTRIFUGATION;

EID: 0346733333     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03383004     Document Type: Article

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