Literature DB >> 27756047

Visualizing the nanoscale: protein internal dynamics and neutron spin echo spectroscopy.

David Je Callaway1, Zimei Bu2.   

Abstract

The most complex molecular machines are proteins found within cells. Protein dynamics, in particular dynamics on nanoscales, presents us with a novel paradigm for cell signaling: the idea that proteins and protein complexes can communicate directly within themselves to effect long-range information transfer, via coupled domains and correlated residue clusters. This idea has been little explored, in large part because of a paucity of experimental techniques that can address the necessary questions. Here we review recent progress in developing a promising new approach, neutron spin echo spectroscopy.
Copyright © 2016 Elsevier Ltd. All rights reserved.

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Year:  2016        PMID: 27756047      PMCID: PMC5374024          DOI: 10.1016/j.sbi.2016.10.001

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  20 in total

1.  ResiCon: a method for the identification of dynamic domains, hinges and interfacial regions in proteins.

Authors:  Maciej Dziubiński; Paweł Daniluk; Bogdan Lesyng
Journal:  Bioinformatics       Date:  2015-09-05       Impact factor: 6.937

2.  Essential Strategies for Revealing Nanoscale Protein Dynamics by Neutron Spin Echo Spectroscopy.

Authors:  David J E Callaway; Zimei Bu
Journal:  Methods Enzymol       Date:  2015-06-13       Impact factor: 1.600

3.  Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy.

Authors:  Zimei Bu; Ralf Biehl; Michael Monkenbusch; Dieter Richter; David J E Callaway
Journal:  Proc Natl Acad Sci U S A       Date:  2005-11-23       Impact factor: 11.205

4.  Nanoscale protein dynamics: a new frontier for neutron spin echo spectroscopy.

Authors:  David J E Callaway; Bela Farago; Zimei Bu
Journal:  Eur Phys J E Soft Matter       Date:  2013-07-17       Impact factor: 1.890

5.  Nanoscale protein domain motion and long-range allostery in signaling proteins- a view from neutron spin echo sprectroscopy.

Authors:  David J E Callaway; Zimei Bu
Journal:  Biophys Rev       Date:  2015-06

6.  Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase.

Authors:  Liang Hong; Melissa A Sharp; Simón Poblete; Ralf Biehl; Michaela Zamponi; Noemi Szekely; Marie-Sousai Appavou; Roland G Winkler; Rachel E Nauss; Alexander Johs; Jerry M Parks; Zheng Yi; Xiaolin Cheng; Liyuan Liang; Michael Ohl; Susan M Miller; Dieter Richter; Gerhard Gompper; Jeremy C Smith
Journal:  Biophys J       Date:  2014-07-15       Impact factor: 4.033

7.  Allostery without conformational change. A plausible model.

Authors:  A Cooper; D T Dryden
Journal:  Eur Biophys J       Date:  1984       Impact factor: 1.733

8.  Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1.

Authors:  Jianquan Li; David J E Callaway; Zimei Bu
Journal:  J Mol Biol       Date:  2009-07-08       Impact factor: 5.469

9.  EPAC1 activation by cAMP stabilizes CFTR at the membrane by promoting its interaction with NHERF1.

Authors:  Miguel J Lobo; Margarida D Amaral; Manuela Zaccolo; Carlos M Farinha
Journal:  J Cell Sci       Date:  2016-05-20       Impact factor: 5.285

10.  Neutron spin-echo studies of hemoglobin and myoglobin: multiscale internal dynamics.

Authors:  Jyotsana Lal; Peter Fouquet; Marco Maccarini; Lee Makowski
Journal:  J Mol Biol       Date:  2010-01-22       Impact factor: 5.469

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  4 in total

1.  Dynamic structure of the full-length scaffolding protein NHERF1 influences signaling complex assembly.

Authors:  Shibani Bhattacharya; Christopher B Stanley; William T Heller; Peter A Friedman; Zimei Bu
Journal:  J Biol Chem       Date:  2019-06-06       Impact factor: 5.157

2.  Activated nanoscale actin-binding domain motion in the catenin-cadherin complex revealed by neutron spin echo spectroscopy.

Authors:  Bela Farago; Iain D Nicholl; Shen Wang; Xiaolin Cheng; David J E Callaway; Zimei Bu
Journal:  Proc Natl Acad Sci U S A       Date:  2021-03-30       Impact factor: 11.205

3.  α-Catenin Structure and Nanoscale Dynamics in Solution and in Complex with F-Actin.

Authors:  Iain D Nicholl; Tsutomu Matsui; Thomas M Weiss; Christopher B Stanley; William T Heller; Anne Martel; Bela Farago; David J E Callaway; Zimei Bu
Journal:  Biophys J       Date:  2018-07-11       Impact factor: 4.033

4.  Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics.

Authors:  David J E Callaway; Tsutomu Matsui; Thomas Weiss; Laura R Stingaciu; Christopher B Stanley; William T Heller; Zimei Bu
Journal:  J Mol Biol       Date:  2017-03-08       Impact factor: 5.469

  4 in total

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