The A-kinase Anchoring Domain of Type IIα cAMP-dependent Protein Kinase Is Highly Helical
Open Access
- 1 September 1997
- journal article
- Published by Elsevier
- Vol. 272 (38) , 23637-23644
- https://doi.org/10.1074/jbc.272.38.23637
Abstract
No abstract availableKeywords
This publication has 63 references indexed in Scilit:
- Protein kinase C: Ports of anchor in the cellCurrent Biology, 1996
- 1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 1995
- Stabilization of a type VI turn in a family of linear peptides in water solutionJournal of Molecular Biology, 1994
- Signal transduction through the cAMP-dependent protein kinaseMolecular and Cellular Biochemistry, 1993
- Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signalBiochemistry, 1993
- Blotting and band-shifting: techniques for studying protein-protein interactionsTrends in Biochemical Sciences, 1992
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Improved three-dimensional1H−13C−1H correlation spectroscopy of a13C-labeled protein using constant-time evolutionJournal of Biomolecular NMR, 1991
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Proline‐containing β‐turns in peptides and proteins. II. Physicochemical studies on tripeptides with the Pro‐Gly sequenceBiopolymers, 1982