CONFORMATIONAL AND BINDING-STUDIES ON PEPTIDES RELATED TO DOMAIN-I AND DOMAIN-III OF CALMODULIN

被引：6

作者：

FOFFANI, MT ^{[1
]}

BATTISTUTTA, R ^{[1
]}

CALDERAN, A ^{[1
]}

RUZZA, P ^{[1
]}

BORIN, G ^{[1
]}

PEGGION, E ^{[1
]}

机构：

[1] UNIV PADUA,BIOPOLYMER RES CTR,DEPT ORGAN CHEM,VIA MARZOLO 1,I-35131 PADUA,ITALY

来源：

BIOPOLYMERS | 1991年 / 31卷 / 06期

关键词：

D O I：

10.1002/bip.360310612

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：

The conformational and ion-binding properties of two peptide fragments of 25 amino acid residues corresponding to the helix-loop sequences of domains I and III of calmodulin (CaM) were investigated by CD and Tb3+ -mediated fluorescence spectroscopy. Both peptides exhibit very similar ion binding properties either in water or trifluoroethanol (TFE), and do not allow the differentiation of the two domains in the native protein in terms of their binding capacity. An aggregation phenomenon was observed in TFE with increase of the alpha-helical content. We suggest that the aggregation involves an interaction between the hydrophilic surfaces of amphiphilic alpha-helices in a way similar to inverse micelle formation.

引用

页码：671 / 681

页数：11

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