Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin-1

被引：18

作者：

Dames, SA

Kammerer, RA

Moskau, D

Engel, J

Alexandrescu, AT ^{[1
]}

机构：

[1] Univ Basel, Biozentrum, Dept Biol Struct, CH-4056 Basel, Switzerland

[2] Univ Basel, Biozentrum, Dept Biophys Chem, CH-4056 Basel, Switzerland

[3] Bruker AG, CH-8117 Faellanden, Switzerland

来源：

FEBS LETTERS | 1999年 / 446卷 / 01期

关键词：

cartilage matrix protein; ion pair; salt bridge; electrostatic; stability; specificity; ionization constant;

D O I：

10.1016/S0014-5793(99)00186-6

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 pK(a) values of eight glutamic acid residues in the homotrimeric coiled coil domain of chicken matrilin-1 have been determined from 2D H(CA)CO NMR spectra recorded as a function of the solution pH. The pK(a) values span a range between 4.0 and 4.7, close to or above those for glutamic acid residues in unstructured polypeptides. These results suggest only small favorable contributions to the stability of the coiled coil from the ionization of its acidic residues. (C) 1999 Federation of European Biochemical Societies.

引用

页码：75 / 80

页数：6

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