Aggregation of chymotrypsinogen: portrait by infrared spectroscopy.
Biochim Biophys Acta
; 1121(1-2): 183-8, 1992 May 22.
Article
em En
| MEDLINE
| ID: mdl-1599940
ABSTRACT
Changes in the secondary structure and aggregation of chymotrypsinogen were investigated by infrared difference spectroscopy in conjunction with temperature and pressure tuning IR spectroscopy; both the amide I' band and side chain bands were studied. A prominent component of the amide I' band in the difference spectrum obtained upon cooling a chymotrypsinogen solution, or increasing the hydrostatic pressure, was observed in the region between 1627 and 1622 cm-1. Under denaturing conditions a white gel was formed, which is attributed to irreversible self-association or aggregation. This process was accompanied by the appearance of two new amide I' bands in the infrared spectrum of the protein a very strong band at 1618 cm-1 and a weak band at 1685 cm-1. These bands are assigned to peptide segments with anti-parallel aligned beta-strands.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Quimotripsinogênio
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1992
Tipo de documento:
Article