Binding of alkylsulfonate ligands to bovine β-lactoglobulin: Effects on protein denaturation by urea

Food Hydrocolloids

Volumn 19, Issue 2, 2005, Pages 249-255

  Busti, Pablo ^a   Scarpeci, Sonia ^a   Gatti, Carlos A ^a   Delorenzi, Néstor J ^a  

^a Fis Fac Cie Bioquimicas Y F   (Argentina)

Author keywords

Beta lactoglobulin; Chemical unfolding by urea; Dissociation coupled unfolding (DCU) model; Fluorescence spectroscopy; Hydrophobic binding sites

Indexed keywords

AMINO ACIDS; BINDING SITES; DENATURATION; DIMERS; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; LIGANDS; MAMMALS; METABOLISM; MONOMERS; PROTEINS; UREA;

BETA-LACTOGLOBULIN; BINDING-SITES; BOVINE Β-LACTOGLOBULIN; CHEMICAL UNFOLDING BY UREA; DISSOCIATION COUPLED UNFOLDING MODEL; HYDROPHOBIC BINDING; HYDROPHOBIC BINDING SITE; LIGAND BINDING; UNFOLDING MODELS; UNFOLDINGS;

DISSOCIATION;

ALKANESULFONIC ACID DERIVATIVE; LACTOGLOBULIN; UREA;

ARTICLE; BINDING SITE; FLUORESCENCE; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR MODEL; PH MEASUREMENT; PROTEIN DENATURATION; PROTEIN INTERACTION; RIGIDITY;

BOVINAE;

EID: 8644272468     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2004.05.007     Document Type: Article

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