Characterization of the unfolded state of bovine α-lactalbumin and comparison with unfolded states of homologous proteins

Protein Science

Volumn 15, Issue 6, 2006, Pages 1397-1407

  Wirmer, Julia ^a,b   Berk, Holger ^a   Ugolini, Raffaella ^c   Redfield, Christina ^c   Schwalbe, Harald ^a  

^a GOETHE UNIVERSITY   (Germany)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

lactalbumin; Lysozyme; NMR spectroscopy; Protein folding; Unfolded proteins

Indexed keywords

ALPHA LACTALBUMIN; CALCIUM BINDING PROTEIN; LYSOZYME;

AMINO ACID SEQUENCE; ARTICLE; COW; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CATTLE; CHICKENS; CONSERVED SEQUENCE; HUMANS; HYDROPHOBICITY; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMIDASE; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN;

BOS TAURUS;

EID: 33744470104     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051974506     Document Type: Article

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