ArticleBiochemistry2008
Monitoring aromatic picosecond to nanosecond dynamics in proteins via 13C relaxation: expanding perturbation mapping of the rigidifying core mutation, V54A, in eglin c.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins.The journal of physical chemistry. B · 2023Review
- Article
- Conformational exchange of aromatic side chains byJournal of biomolecular NMR · 2018Article
- Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase.Journal of structural biology · 2017Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
- Networks of Dynamic Allostery Regulate Enzyme Function.Structure (London, England : 1993) · 2017Article
- Bacterial production of site specificJournal of biomolecular NMR · 2017Article
- Recapturing the Correlated Motions of Protein Using Coarse- Grained Models.Protein and peptide letters · 2015Article
- Prepaying the entropic cost for allosteric regulation in KIX.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection.Journal of biomolecular NMR · 2014Article
- A 13C labeling strategy reveals a range of aromatic side chain motion in calmodulin.Journal of the American Chemical Society · 2013Article
- ¹³C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy.Journal of biomolecular NMR · 2012Article
- Structure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complex.PloS one · 2012Article
- Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.PLoS computational biology · 2012Article
- An upper limit for macromolecular crowding effects.BMC biophysics · 2011Article
- Exploring the role of structure and dynamics in the function of chymotrypsin inhibitor 2.Proteins · 2011Article
- Detection of native-state nonadditivity in double mutant cycles via hydrogen exchange.Journal of the American Chemical Society · 2010Article
- Intrinsic domain and loop dynamics commensurate with catalytic turnover in an induced-fit enzyme.Structure (London, England : 1993) · 2009Article
- Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima.Journal of biomolecular NMR · 2009Article
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2 authors.
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Abstract
Long-range effects, such as allostery, have evolved in proteins as a means of regulating function via communication between distal sites. An NMR-based perturbation mapping approach was used to more completely probe the dynamic response of the core mutation V54A in the protein eglin c by monitoring changes in picosecond to nanosecond aromatic side-chain dynamics and H/D exchange stabilities. Previous side-chain dynamics studies on this mutant were limited to methyl-bearing residues, most of which were found to rigidify on the picosecond to nanosecond time scale in the form of a contiguous "network". Here, high precision (13)C relaxation data from 13 aromatic side chains were acquired by applying canonical relaxation experiments to a newly developed carbon labeling scheme [Teilum et al. (2006) J. Am. Chem. Soc. 128, 2506-2507]. The fitting of model-free parameters yielded S (2) variability which is intermediate with respect to backbone and methyl-bearing side-chain variability and tau e values that are approximately 1 ns. Inclusion of the aromatic dynamic response results in an expanded network of dynamically coupled residues, with some aromatics showing increases in flexibility, which partially offsets the rigidification in methyl side chains. Using amide hydrogen exchange, dynamic propagation on a slower time scale was probed in response to the V54A perturbation. Surprisingly, regional stabilization (slowed exchange) 10-12 A from the site of mutation was observed despite a global destabilization of 1.5 kcal x mol (-1). Furthermore, this unlikely pocket of stabilized residues colocalizes with increases in aromatic flexibility on the faster time scale. Because the converse is also true (destabilized residues colocalize with rigidification on the fast time scale), a plausible entropy-driven mechanism is discussed for relating colocalization of opposing dynamic trends on vastly different time scales.
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