AGGREGATION OF CHYMOTRYPSINOGEN - PORTRAIT BY INFRARED-SPECTROSCOPY

被引：179

作者：

ISMAIL, AA

MANTSCH, HH

WONG, PTT

机构：

[1] Steacie Institute for Molecular Sciences, National Research Council of Canada, Ottawa

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1121卷 / 1-2期

关键词：

HIGH PRESSURE; TEMPERATURE; PROTEIN; AGGREGATION; SECONDARY STRUCTURE; INFRARED SPECTROSCOPY; DENATURATION;

D O I：

10.1016/0167-4838(92)90353-F

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：183 / 188

页数：6

共 16 条

[1] INVESTIGATION OF ADENYLATE KINASE FROM ESCHERICHIA-COLI AND ITS INTERACTION WITH NUCLEOTIDES BY FOURIER-TRANSFORM INFRARED-SPECTROSCOPY [J].