Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2

FEBS Letters

Volumn 436, Issue 2, 1998, Pages 149-154

  Fogolari, F ^a   Ragona, L ^b   Zetta, L ^b   Romagnoli, S ^a   De Kruif, K G ^c   Molinari, H ^a  

^a UNIVERSITY OF VERONA   (Italy)

^b CNR   (Italy)

^c NIZO FOOD RESEARCH   (Netherlands)

Author keywords

Bovine lactoglobulin; Nuclear magnetic resonance; Structure calculation; Surface electrostatic property

Indexed keywords

BETA LACTOGLOBULIN;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; IONIC STRENGTH; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; SURFACE CHARGE; X RAY CRYSTALLOGRAPHY;

ALGORITHMS; AMINO ACID SEQUENCE; ANIMALS; APOPROTEINS; CATTLE; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; LACTOGLOBULINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

BOVINAE;

EID: 0032475891     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)00936-3     Document Type: Article

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