Chemical synthesis and structure elucidation of bovine kappa-casein (1-44)
Contribuinte(s) |
W. Baumeister E. Carafoli C.H. Chung A. Goffeau J.D. Jamieson C.B. Klee M.D. Lane W.J. Lennarz M.Muramatsu |
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Data(s) |
01/01/2006
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Resumo |
The caseins (alpha(s1), alpha(s2), beta, and kappa) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1-44) of bovine K-casein, the protein which maintains the micellar structure of the caseins. K-Casein (1-44) was synthesised by highly optimised Boc solid-phase peptide chemistry and characterised by mass spectrometry. Structure elucidation was carried out by circular dichroism and nuclear magnetic resonance spectroscopy. CD analysis demonstrated that the segment was ill defined in aqueous medium but in 30% trifluoroethanol it exhibited considerable helical structure. Further, NMR analysis showed the presence of a helical segment containing 26 residues which extends from Pro(8) to Arg(34). This is the first report which demonstrates extensive secondary structure within the casein class of proteins. (c) 2006 Elsevier Inc. All rights reserved. |
Identificador | |
Idioma(s) |
eng |
Publicador |
Academic Press Inc Elsevier Science |
Palavras-Chave | #Solid-phase Peptide Synthesis #2d Nmr #Milk Protein #Kappa-casein #Helical Structure #Biochemistry & Molecular Biology #Biophysics #Nuclear-magnetic-resonance #Nmr-spectroscopy #Secondary Structures #Proteins #Micelle #Peptide #Technology #Assignment #Chymosin #C1 #250302 Biological and Medical Chemistry #780105 Biological sciences #780103 Chemical sciences |
Tipo |
Journal Article |