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

Authors
Dames, SA Kammerer, RA Moskau, D Engel, J Alexandrescu, AT
Citation
Sa. Dames et al., Contributions of the ionization states of acidic residues to the stabilityof the coiled coil domain of matrilin-1, FEBS LETTER, 446(1), 1999, pp. 75-80
Citations number
29
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
446
Issue
1
Year of publication
1999
Pages
75 - 80
Database
ISI
SICI code
0014-5793(19990305)446:1<75:COTISO>2.0.ZU;2-M
Abstract
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 resid ues in unstructured polypeptides. These results suggest only small favorabl e contributions to the stability of the coiled coil from the ionization of its acidic residues. (C) 1999 Federation of European Biochemical Societies.