Literature DB >> 10100618

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

S A Dames1, R A Kammerer, D Moskau, J Engel, A T Alexandrescu.   

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.

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Year:  1999        PMID： 10100618     DOI： 10.1016/s0014-5793(99)00186-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  4 in total

1.  Molecular basis of coiled-coil formation.

Authors:  Michel O Steinmetz; Ilian Jelesarov; William M Matousek; Srinivas Honnappa; Wolfgang Jahnke; John H Missimer; Sabine Frank; Andrei T Alexandrescu; Richard A Kammerer
Journal:  Proc Natl Acad Sci U S A       Date:  2007-04-16       Impact factor: 11.205

2.  NMR determination of pKa values in α-synuclein.

Authors:  Robyn L Croke; Sharadrao M Patil; Jason Quevreaux; Debra A Kendall; Andrei T Alexandrescu
Journal:  Protein Sci       Date:  2010-12-13       Impact factor: 6.725

3.  Electrostatic contributions to the stability of the GCN4 leucine zipper structure.

Authors:  William M Matousek; Barbara Ciani; Carolyn A Fitch; Bertrand Garcia-Moreno; Richard A Kammerer; Andrei T Alexandrescu
Journal:  J Mol Biol       Date:  2007-09-11       Impact factor: 5.469

4.  Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix.

Authors:  Anne R Kaplan; Megan R Brady; Mark W Maciejewski; Richard A Kammerer; Andrei T Alexandrescu
Journal:  Biochemistry       Date:  2017-03-09       Impact factor: 3.162
  4 in total

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