Work

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

Year: 1999

Type: article

Abstract: 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.

Source: FEBS Letters

DOI: 10.1016/s0014-5793(99)00186-6

Authors: Sonja A. Dames, Richard A. Kammerer, Detlef Moskau, Jürgen Engel, Andrei T. Alexandrescu

Institutions: University of Basel, Bruker (Switzerland)

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Science Foundation, Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

OpenAlex ID: W2067218309

FWCI: 0.799

Cites: 29

Cited by: 19

Related to: 10