High-Resolution Triple-Resonance NMR Spectroscopy of a Novel Calmodulin·Peptide Complex at Kilobar Pressures
- 13 November 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (45) , 11329-11330
- https://doi.org/10.1021/ja962552g
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Molecular Recognition by Calmodulin: Pressure-Induced Reorganization of a Novel Calmodulin−Peptide ComplexBiochemistry, 1996
- Energetics and dynamics of molecular recognition by calmodulinBiochemistry, 1995
- Structural Analysis of a Novel Interaction by Calmodulin: High-Affinity Binding of a Peptide in the Absence of CalciumBiochemistry, 1995
- Role of hydrophobic and hydrophilic forces in peptide-protein interaction: New advancesPeptides, 1995
- High-Pressure NMR Spectroscopy of Proteins and MembranesAnnual Review of Biophysics, 1994
- Calmodulin interacts with amphiphilic peptides composed of all D-amino acidsNature, 1994
- Carbon-hydrogen insertions in the reactions of Fischer carbene complexes with ketene acetalsJournal of the American Chemical Society, 1992
- Role of extracellular disulfide-bonded cysteines in the ligand binding function of the .beta.2-adrenergic receptorBiochemistry, 1990
- How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helicesTrends in Biochemical Sciences, 1990
- Activation volumes for the rotational motion of interior aromatic rings in globular proteins determined by high resolution 1H NMR at variable pressureFEBS Letters, 1980