ArticleBiophysical journal2008
Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residues.
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 14 papers.
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Who cites it
14 citing papers in PubMed.
- Using Cross-Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
- Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Review
- Cross-correlated relaxation rates between protein backbone H-X dipolar interactions.Journal of biomolecular NMR · 2017Article
- Direct Investigation of Slow Correlated Dynamics in Proteins via Dipolar Interactions.Journal of the American Chemical Society · 2016Article
- Characterizing a partially ordered miniprotein through folding molecular dynamics simulations: Comparison with the experimental data.Protein science : a publication of the Protein Society · 2016Article
- The unusual internal motion of the villin headpiece subdomain.Protein science : a publication of the Protein Society · 2016Article
- (15)N CSA tensors and (15)N-(1)H dipolar couplings of protein hydrophobic core residues investigated by static solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Glassy dynamics of protein methyl groups revealed by deuteron NMR.The journal of physical chemistry. B · 2013Article
- Article
- Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain.Journal of biomolecular NMR · 2011Article
- Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant.Journal of biomolecular NMR · 2010Article
- An unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomain.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Phosphorylation-induced changes in backbone dynamics of the dematin headpiece C-terminal domain.Journal of biomolecular NMR · 2009Article
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2 authors.
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Abstract
The villin headpiece subdomain (HP36) is a widely used system for protein-folding studies. Nuclear magnetic resonance cross-correlated relaxation rates arising from correlated fluctuations of two N-H(N) dipole-dipole interactions involving successive residues were measured at two temperatures at which HP36 is at least 99% folded. The experiment revealed the presence of motions slower than overall tumbling of the molecule. Based on the theoretical analysis of the spectral densities we show that the structural and dynamic contributions to the experimental cross-correlated relaxation rate can be separated under certain conditions. As a result, dynamic cross-correlated order parameters describing slow microsecond-to-millisecond motions of N-H bonds in neighboring residues can be introduced for any extent of correlations in the fluctuations of the two bond vectors. These dynamic cross-correlated order parameters have been extracted for HP36. The comparison of their values at two different temperatures indicates that when the temperature is raised, slow motions increase in amplitude. The increased amplitude of these fluctuations may reflect the presence of processes directly preceding the unfolding of the protein.
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