Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Academic Article

abstract

• The response of the internal dynamics of calcium-saturated calmodulin to the formation of a complex with a peptide model of the calmodulin-binding domain of the smooth muscle myosin light chain kinase has been studied using NMR relaxation methods. The backbone of calmodulin is found to be unaffected by the binding of the domain, whereas the dynamics of side chains are significantly perturbed. The changes in dynamics are interpreted in terms of a heterogeneous partitioning between structure (enthalpy) and dynamics (entropy). These data provide a microscopic view of the residual entropy of a protein in two functional states and suggest extensive enthalpy/entropy exchange during the formation of a protein-protein interface.

authors

• Wand, Joshua

published proceedings

• Nat Struct Biol

author list (cited authors)

• Lee, A. L., Kinnear, S. A., & Wand, A. J.

citation count

• 320

complete list of authors

• Lee, AL||Kinnear, SA||Wand, AJ

publication date

• January 2000

publisher

• Springer Nature  Publisher

published in

• Nature Structural and Molecular Biology  Journal

keywords

• Amino Acid Sequence
• Animals
• Binding Sites
• Calcium
• Calmodulin
• Chickens
• Entropy
• Kinetics
• Magnetic Resonance Spectroscopy
• Models, Molecular
• Molecular Sequence Data
• Muscle, Smooth
• Myosin-Light-Chain Kinase
• Peptide Fragments
• Pliability
• Protein Binding
• Protein Conformation
• Thermodynamics
• Water

PubMed Central ID

• 10625431

Digital Object Identifier (DOI)

• 10.1038/71280

start page

• 72

end page

• 77

volume

• 7

issue

• 1

URL

• http://dx.doi.org/10.1038/71280