Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase
- 1 October 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (40) , 9316-9324
- https://doi.org/10.1021/bi00492a003
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 21 references indexed in Scilit:
- Comparison of the crystal and solution structures of calmodulin and troponin CBiochemistry, 1988
- NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriationBiochemistry, 1988
- Crosslinking of rabbit skeletal muscle troponin with the photoactive reagent 4-maleimidobenzophenone: identification of residues in troponin I that are close to cysteine-98 of troponin CBiochemistry, 1987
- Calmodulin and troponin C: a comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]Biochemistry, 1986
- Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle x-ray scatteringBiochemistry, 1985
- Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase.Proceedings of the National Academy of Sciences, 1985
- Three-dimensional structure of calmodulinNature, 1985
- Phosphorylase Kinase from Rabbit Skeletal Muscle Identification of the Calmodulin‐Binding SubunitsEuropean Journal of Biochemistry, 1980
- Structural similarities between the Ca2+-dependent regulatory proteins of 3':5'-cyclic nucleotide phosphodiesterase and actomyosin ATPase.Journal of Biological Chemistry, 1976
- La diffraction des rayons X aux très petits angles : application à l'étude de phénomènes ultramicroscopiquesAnnales de Physique, 1939