Equilibrium unfolding cd studies of bovine β-lactoglobulin and its 14- 52 fragment at acidic pH

Biopolymers

Volumn 49, Issue 6, 1999, Pages 441-450

  Ragona, L ^a   Confalonieri, L ^a   Zetta, L ^a   De Kruif, K G ^b   Mammi, S ^c   Peggion, E ^c   Longhi, R ^a   Molinari, Henriette ^d,e  

^a CNR   (Italy)

^b NIZO FOOD RESEARCH   (Netherlands)

^c UNIVERSITY OF PADOVA   (Italy)

^d UNIVERSITY OF VERONA   (Italy)

^e Istituto Policattedra   (Italy)

Author keywords

lactoglobulin; CD; Locally unfolded structure; Urea unfolding

Indexed keywords

BIOSYNTHESIS; CONFORMATIONS; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; ORGANIC SOLVENTS; PH EFFECTS; UREA;

BOVINE LACTOGLOBULIN; EQUILIBRIUM UNFOLDING;

PROTEINS;

BETA LACTOGLOBULIN; UREA;

ACIDITY; ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CATTLE; CIRCULAR DICHROISM; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TRANSLATION INITIATION;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; LACTOGLOBULINS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; UREA;

BOS TAURUS; BOVINAE;

EID: 0033135870     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0282(199905)49:6<441::AID-BIP2>3.0.CO;2-A     Document Type: Article

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