Literature DB >> 19846313

Observing biological dynamics at atomic resolution using NMR.

Anthony K Mittermaier1, Lewis E Kay.   

Abstract

Biological macromolecules are highly flexible and continually undergo conformational fluctuations on a broad spectrum of timescales. It has long been recognized that dynamics have an important role in the action of these molecules. However, the relationship between molecular function and motion is extremely challenging to delineate, because the conformational space available to macromolecules is vast and the relevant excursions can be infrequent and short-lived. Recent advances in solution nuclear magnetic resonance (NMR) spectroscopy permit biomolecular dynamics to be observed with unprecedented detail. Applications of these new NMR techniques to the study of fundamental processes such as binding and catalysis have provided new insights into how living systems operate at an atomic level.

Mesh:

Substances:

Year:  2009        PMID: 19846313     DOI: 10.1016/j.tibs.2009.07.004

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  133 in total

Review 1.  Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopy.

Authors:  Hassane S McHaourab; P Ryan Steed; Kelli Kazmier
Journal:  Structure       Date:  2011-11-09       Impact factor: 5.006

2.  Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.

Authors:  Carlo Camilloni; Daniel Schaal; Kristian Schweimer; Stephan Schwarzinger; Alfonso De Simone
Journal:  Biophys J       Date:  2012-01-03       Impact factor: 4.033

3.  Intrinsic disorder modulates protein self-assembly and aggregation.

Authors:  Alfonso De Simone; Craig Kitchen; Ann H Kwan; Margaret Sunde; Christopher M Dobson; Daan Frenkel
Journal:  Proc Natl Acad Sci U S A       Date:  2012-04-16       Impact factor: 11.205

4.  Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.

Authors:  Alexander I Greenwood; Monique J Rogals; Soumya De; Kun Ping Lu; Evgenii L Kovrigin; Linda K Nicholson
Journal:  J Biomol NMR       Date:  2011-09-27       Impact factor: 2.835

5.  Transiently populated intermediate functions as a branching point of the FF domain folding pathway.

Authors:  Dmitry M Korzhnev; Tomasz L Religa; Lewis E Kay
Journal:  Proc Natl Acad Sci U S A       Date:  2012-05-30       Impact factor: 11.205

6.  An exciting but challenging road ahead for computational enzyme design.

Authors:  David Baker
Journal:  Protein Sci       Date:  2010-10       Impact factor: 6.725

7.  Structural biology: Proteins in dynamic equilibrium.

Authors:  Pau Bernadó; Martin Blackledge
Journal:  Nature       Date:  2010-12-23       Impact factor: 49.962

8.  High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.

Authors:  John McCoy; Wayne L Hubbell
Journal:  Proc Natl Acad Sci U S A       Date:  2011-01-04       Impact factor: 11.205

9.  (19)F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus.

Authors:  James M Aramini; Keith Hamilton; Li-Chung Ma; G V T Swapna; Paul G Leonard; John E Ladbury; Robert M Krug; Gaetano T Montelione
Journal:  Structure       Date:  2014-02-27       Impact factor: 5.006

10.  Evaluating the uncertainty in exchange parameters determined from off-resonance R1ρ relaxation dispersion for systems in fast exchange.

Authors:  Jameson R Bothe; Zachary W Stein; Hashim M Al-Hashimi
Journal:  J Magn Reson       Date:  2014-04-20       Impact factor: 2.229

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.