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Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin‐1
Author(s) -
Dames Sonja A.,
Kammerer Richard A.,
Moskau Detlef,
Engel Jürgen,
Alexandrescu Andrei T.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00186-6
Subject(s) - coiled coil , glutamic acid , chemistry , ionization , amino acid residue , amino acid , crystallography , stereochemistry , peptide sequence , biochemistry , organic chemistry , ion , gene
The p K 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 p K 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.