Comparison of the conformational stability of the non-native α-helical intermediate of thiol-modified β-lactoglobulin upon interaction with sodium n-alkyl sulfates at two different pH

Journal of Colloid and Interface Science

Volumn 299, Issue 2, 2006, Pages 636-646

  Chamani, J ^a  

^a ISLAMIC AZAD UNIVERSITY   (Iran)

Author keywords

Alpha helix; Hydrophobicity; n Alkyl sulfates; Non hierarchical folding; Non native alpha helical; TNB LG

Indexed keywords

HYDROPHOBICITY; MONOMERS; PROTEINS; SODIUM COMPOUNDS; STABILITY;

ALPHA-HELIX; N-ALKYL SULFATES; NON-HIERARCHICAL FOLDING; NON-NATIVE ALPHA-HELICAL; TNB-Β-LG;

ALCOHOLS;

5,5' DITHIOBIS(2 NITROBENZOIC ACID); BETA LACTOGLOBULIN; DODECYL SULFATE SODIUM; NITROBENZOIC ACID DERIVATIVE; SULFATE; TETRADECYL SULFATE SODIUM; THIOL DERIVATIVE;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; COMPARATIVE STUDY; CONFORMATION; DIFFERENTIAL SCANNING CALORIMETRY; DISULFIDE BOND; FLUORESCENCE; HYDROPHOBICITY; PH; PRIORITY JOURNAL; PROTEIN FOLDING;

ANIMALS; CATTLE; CIRCULAR DICHROISM; DITHIONITROBENZOIC ACID; DRUG STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOGLOBULINS; MOLECULAR CONFORMATION; SODIUM; SPECTROPHOTOMETRY; SULFURIC ACID ESTERS;

EID: 33646902188     PISSN: 00219797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jcis.2006.02.049     Document Type: Article

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