[Self-association and secondary structure of beta-casein].
Bioorg Khim
; 39(4): 411-7, 2013.
Article
em Ru
| MEDLINE
| ID: mdl-24707721
ABSTRACT
The secondary structure alterations, accompanying isothermal and temperature guided beta-casein micellization have been studied by dynamic light scattering, circular dichroism and Fourier transform infrared spectroscopy techniques. Micelle formation induced by increase of protein concentration at constant temperature is accompanied by the formation of scanty number of additional peptide hydrogen bonds, preliminary assigned to intraprotein beta-structure. Heating results in more pronounced but qualitatively different changes consisted in dehydration of peptide groups and disruption of polyproline II helix segments with subsequent conversion to random and beta-turns. Nevertheless, in both cases the total number of residues involved in transition is quite few and cannot be regarded as a decisive factor for casein micellization.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Caseínas
/
Estrutura Secundária de Proteína
/
Proteínas do Leite
Tipo de estudo:
Risk_factors_studies
Limite:
Animals
Idioma:
Ru
Ano de publicação:
2013
Tipo de documento:
Article