Complete assignment of 1H, 13C and 15N chemical shifts for bovine β-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form

Journal of Biomolecular NMR

Volumn 12, Issue 1, 1998, Pages 89-107

  Uhrínová, Stanislava ^a   Uhrín, Dušan ^a   Denton, Helen ^b,d   Smith, Mark ^c   Sawyer, Lindsay ^b   Barlow, Paul N ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b Structural Biochemistry Group   (United Kingdom)

^c NEW ZEALAND DAIRY RESEARCH INSTITUTE   (New Zealand)

^d DURHAM UNIVERSITY   (United Kingdom)

Author keywords

Methyl containing residues; Modified HCCH TOCSY; Partially folded form; Side chain assignment; lactoglobulin

Indexed keywords

BOVINAE; PICHIA PASTORIS;

CARBON; HYDROGEN; LACTOGLOBULIN; NITROGEN; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CATTLE; CHEMISTRY; COMPARATIVE STUDY; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; CARBON ISOTOPES; CATTLE; CRYSTALLOGRAPHY, X-RAY; HYDROGEN; LACTOGLOBULINS; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 0032110129     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1008268528695     Document Type: Article

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