Partially folded structure of monomeric bovine beta-lactoglobulin.
Bovine beta-LG (beta-lactoglobulin) has been studied under a variety of solution conditions by one- and two-dimensional NMR spectroscopy. At highly acidic pH (pH=2) and low ionic strength the protein is present in a monomeric form, exhibiting a highly structured beta-sheet core and less ordered regions as evidenced by both CD data and the NOESY spectra. Marginal protection was observed for most of the amide protons as a result of high conformational mobility. This structural state of beta-LG may be considered as an attractive model for a partially folded structure occurring late in the folding process of the protein.
Molinari
H
H
Istituto Policattedra della Facoltà di Scienze, Universitá degli Studidi Verona, Italy.
Ragona
L
L
Varani
L
L
Musco
G
G
Consonni
R
R
Zetta
L
L
Monaco
H L
HL
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D005260:Female; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008892:Milk; D008969:Molecular Sequence Data; D009994:Osmolar Concentration; D017510:Protein Folding
D007782:Lactoglobulins