Literature DB >> 10834833

How soft is a protein? A protein dynamics force constant measured by neutron scattering.

G Zaccai1.   

Abstract

An effective environmental force constant is introduced to quantify the molecular resilience (or its opposite, "softness") of a protein structure and relate it to biological function and activity. Specific resilience-function relations were found in neutron-scattering experiments on purple membranes containing bacteriorhodopsin, the light-activated proton pump of halobacteria; the connection between resilience and stability is illustrated by a study of myoglobin in different environments. Important advantages of the neutron method are that it can characterize the dynamics of any type of biological sample-which need not be crystalline or monodisperse-and that it enables researchers to focus on the dynamics of specific parts of a complex structure with deuterium labeling.

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Year:  2000        PMID: 10834833     DOI: 10.1126/science.288.5471.1604

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  169 in total

1.  Anisotropy of fluctuation dynamics of proteins with an elastic network model.

Authors:  A R Atilgan; S R Durell; R L Jernigan; M C Demirel; O Keskin; I Bahar
Journal:  Biophys J       Date:  2001-01       Impact factor: 4.033

2.  Protein flexibility from the dynamical transition: a force constant analysis.

Authors:  D J Bicout; G Zaccai
Journal:  Biophys J       Date:  2001-03       Impact factor: 4.033

3.  Radially softening diffusive motions in a globular protein.

Authors:  S Dellerue; A J Petrescu; J C Smith; M C Bellissent-Funel
Journal:  Biophys J       Date:  2001-09       Impact factor: 4.033

4.  Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability.

Authors:  M Tehei; D Madern; C Pfister; G Zaccai
Journal:  Proc Natl Acad Sci U S A       Date:  2001-12-04       Impact factor: 11.205

5.  The inverse relationship between protein dynamics and thermal stability.

Authors:  A M Tsai; T J Udovic; D A Neumann
Journal:  Biophys J       Date:  2001-10       Impact factor: 4.033

6.  Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes.

Authors:  M Weik; R B Ravelli; I Silman; J L Sussman; P Gros; J Kroon
Journal:  Protein Sci       Date:  2001-10       Impact factor: 6.725

7.  Stretch-activation and stretch-inactivation of Shaker-IR, a voltage-gated K+ channel.

Authors:  C X Gu; P F Juranka; C E Morris
Journal:  Biophys J       Date:  2001-06       Impact factor: 4.033

8.  Enzymatic conformational fluctuations along the reaction coordinate of cytidine deaminase.

Authors:  Ryan C Noonan; Charles W Carter CW; Carey K Bagdassarian
Journal:  Protein Sci       Date:  2002-06       Impact factor: 6.725

9.  Analysis of protein sequence/structure similarity relationships.

Authors:  Hin Hark Gan; Rebecca A Perlow; Sharmili Roy; Joy Ko; Min Wu; Jing Huang; Shixiang Yan; Angelo Nicoletta; Jonathan Vafai; Ding Sun; Lihua Wang; Joyce E Noah; Samuela Pasquali; Tamar Schlick
Journal:  Biophys J       Date:  2002-11       Impact factor: 4.033

10.  On the importance of atomic fluctuations, protein flexibility, and solvent in ion permeation.

Authors:  Toby W Allen; O S Andersen; Benoit Roux
Journal:  J Gen Physiol       Date:  2004-12       Impact factor: 4.086

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