ArticleBiophysical journal2008
Biophysical study of thermal denaturation of apo-calmodulin: dynamics of native and unfolded states.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Dynamical Behavior of Disordered Regions in Disease-Related Proteins Revealed by Quasielastic Neutron Scattering.Medicina (Kaunas, Lithuania) · 2022Article
- Protein Dimerization via Tyr Residues: Highlight of a Slow Process with Co-Existence of Numerous Intermediates and Final Products.International journal of molecular sciences · 2022Article
- Molecular Dynamics of Lysozyme Amyloid Polymorphs Studied by Incoherent Neutron Scattering.Frontiers in molecular biosciences · 2021Article
- Dioctadecyldimethylammonium bromide, a surfactant model for the cell membrane: Importance of microscopic dynamics.Structural dynamics (Melville, N.Y.) · 2020Review
- Article
- Dynamics of thermodynamically stable, kinetically trapped, and inhibitor-bound states of pepsin.Biophysical journal · 2011Article
- Hemoglobin dynamics in red blood cells: correlation to body temperature.Biophysical journal · 2008Article
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Authors and funding
5 authors.
Funding
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Abstract
Apo-calmodulin, a small, mainly alpha, soluble protein is a calcium-dependent protein activator. This article presents a study of internal dynamics of native and thermal unfolded apo-calmodulin, using quasi-elastic neutron scattering. This technique can probe protein internal dynamics in the picosecond timescale and in the nanometer length-scale. It appears that a dynamical transition is associated with thermal denaturation of apo-calmodulin. This dynamical transition goes together with a decrease of the confinement of hydrogen atoms, a decrease of immobile protons proportion and an increase of dynamical heterogeneity. The comparison of native and unfolded states dynamics suggests that the dynamics of protein atoms is more influenced by their distance to the backbone than by their solvent exposure.
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