Literature DB >> 26932314

Protein dynamics from nuclear magnetic relaxation.

Cyril Charlier1, Samuel F Cousin, Fabien Ferrage.   

Abstract

Nuclear magnetic resonance is a ubiquitous spectroscopic tool to explore molecules with atomic resolution. Nuclear magnetic relaxation is intimately connected to molecular motions. Many methods and models have been developed to measure and interpret the characteristic rates of nuclear magnetic relaxation in proteins. These approaches shed light on a rich and diverse range of motions covering timescales from picoseconds to seconds. Here, we introduce some of the basic concepts upon which these approaches are built and provide a series of illustrations.

Mesh:

Substances:

Year:  2016        PMID: 26932314     DOI: 10.1039/c5cs00832h

Source DB:  PubMed          Journal:  Chem Soc Rev        ISSN: 0306-0012            Impact factor:   54.564


  6 in total

1.  Three-dimensional structure of Megabalanus rosa Cement Protein 20 revealed by multi-dimensional NMR and molecular dynamics simulations.

Authors:  Harini Mohanram; Akshita Kumar; Chandra S Verma; Konstantin Pervushin; Ali Miserez
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2019-09-09       Impact factor: 6.237

Review 2.  Relaxing with liquids and solids - A perspective on biomolecular dynamics.

Authors:  Paul Schanda
Journal:  J Magn Reson       Date:  2019-07-11       Impact factor: 2.229

Review 3.  Molecular dynamics simulations in photosynthesis.

Authors:  Nicoletta Liguori; Roberta Croce; Siewert J Marrink; Sebastian Thallmair
Journal:  Photosynth Res       Date:  2020-04-15       Impact factor: 3.573

4.  Fast evaluation of protein dynamics from deficient 15N relaxation data.

Authors:  Łukasz Jaremko; Mariusz Jaremko; Andrzej Ejchart; Michał Nowakowski
Journal:  J Biomol NMR       Date:  2018-03-28       Impact factor: 2.835

5.  Leveraging the multivalent p53 peptide-MdmX interaction to guide the improvement of small molecule inhibitors.

Authors:  Xiyao Cheng; Rong Chen; Ting Zhou; Bailing Zhang; Zichun Li; Meng Gao; Yongqi Huang; Huili Liu; Zhengding Su
Journal:  Nat Commun       Date:  2022-02-28       Impact factor: 14.919

6.  Structural transitions in Orb2 prion-like domain relevant for functional aggregation in memory consolidation.

Authors:  Javier Oroz; Sara S Félix; Eurico J Cabrita; Douglas V Laurents
Journal:  J Biol Chem       Date:  2020-10-22       Impact factor: 5.157

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.