ArticleJournal of biomolecular NMR2009
Partially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion.
Article in Journal of biomolecular NMR, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- Observation of Arginine Side-Chain Motions Coupled to the Global Conformational Exchange Process in Deubiquitinase A.ACS omega · 2022Article
- Conformational Dynamics of Deubiquitinase A and Functional Implications.Biochemistry · 2021Article
- Analysis of conformational exchange processes using methyl-TROSY-based Hahn echo measurements of quadruple-quantum relaxation.Magnetic resonance (Gottingen, Germany) · 2021Article
- Detection of chemical exchange in methyl groups of macromolecules.Journal of biomolecular NMR · 2019Article
- Chemical Exchange.Methods in enzymology · 2019Article
- Dynamic Response of the C2 Domain of Protein Kinase Cα to CaBiophysical journal · 2016Article
- The unusual internal motion of the villin headpiece subdomain.Protein science : a publication of the Protein Society · 2016Article
- Chemical exchange in biomacromolecules: past, present, and future.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein.Protein science : a publication of the Protein Society · 2014Article
- Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected ¹³C CPMG relaxation dispersion.Journal of biomolecular NMR · 2012Article
- Automated NMR relaxation dispersion data analysis using NESSY.BMC bioinformatics · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
- Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion.Journal of the American Chemical Society · 2010Article
- Selective characterization of microsecond motions in proteins by NMR relaxation.Journal of the American Chemical Society · 2009Article
- A topical issue: NMR investigations of molecular dynamics.Journal of biomolecular NMR · 2009Article
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Authors and funding
7 authors.
Funding
Abstract
Identification and characterization of ensembles of intermediate states remains an important objective in describing protein folding in atomic detail. The 67-residue villin headpiece, HP67, consists of an N-terminal subdomain (residues 10-42) that transiently unfolds at equilibrium under native-like conditions and a highly stable C-terminal subdomain (residues 43-76). The transition between folded and unfolded states of the N-terminal domain has been characterized previously by (15)N NMR relaxation dispersion measurements (Grey et al. in J Mol Biol 355:1078, 2006). In the present work, (13)C spin relaxation was used to further characterize backbone and hydrophobic core contributions to the unfolding process. Relaxation of (13)C(alpha) spins was measured using the Hahn echo technique at five static magnetic fields (11.7, 14.1, 16.4, 18.8, and 21.1 T) and the Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion method at a static magnetic field of 14.1 T. Relaxation of methyl (13)C spins was measured using CPMG relaxation dispersion experiments at static magnetic fields of 14.1 and 18.8 T. Results for (13)C and (15)N spins yielded a consistent model in which the partially unfolded intermediate state of the N-terminal subdomain maintains residual structure for residues near the unprotonated His41 imidazole ring and in the interface between the N- and C-terminal subdomains. In addition, a second faster process was detected that appears to represent local dynamics within the folded state of the molecule and is largely confined to the hydrophobic interface between the N- and C-terminal subdomains.
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