Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin-1.
The pKa 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 pKa 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.
Dames
S A
SA
Department of Structural Biology, Biozentrum, University of Basel, Switzerland.
Kammerer
R A
RA
Moskau
D
D
Engel
J
J
Alexandrescu
A T
AT
D000818:Animals; D004926:Escherichia coli; D016326:Extracellular Matrix Proteins / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D064235:Matrilin Proteins; D011487:Protein Conformation
D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; D064235:Matrilin Proteins