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Protein dynamics as seen by (quasi) elastic neutron scattering

Magazù, S.; Mezei, F. LU ; Falus, Peter; Farago, Bela; Mamontov, E.; Russina, M. and Migliardo, Federica (2017) In Biochimica et Biophysica Acta - General Subjects 1861(1). p.3504-3512
Abstract

Background Elastic and quasielastic neutron scattering studies proved to be efficient probes of the atomic mean square displacement (MSD), a fundamental parameter for the characterization of the motion of individual atoms in proteins and its evolution with temperature and compositional environment. Scope of review We present a technical overview of the different types of experimental situations and the information quasi-elastic neutron scattering approaches can make available. In particular, MSD can crucially depend on the time scale over which the averaging (building of the “mean”) takes place, being defined by the instrumental resolution. Due to their high neutron scattering cross section, hydrogen atoms can be particularly... (More)

Background Elastic and quasielastic neutron scattering studies proved to be efficient probes of the atomic mean square displacement (MSD), a fundamental parameter for the characterization of the motion of individual atoms in proteins and its evolution with temperature and compositional environment. Scope of review We present a technical overview of the different types of experimental situations and the information quasi-elastic neutron scattering approaches can make available. In particular, MSD can crucially depend on the time scale over which the averaging (building of the “mean”) takes place, being defined by the instrumental resolution. Due to their high neutron scattering cross section, hydrogen atoms can be particularly sensitively observed with little interference by the other atoms in the sample. A few examples, including new data, are presented for illustration. Major conclusions The incoherent character of neutron scattering on hydrogen atoms restricts the information obtained to the self-correlations in the motion of individual atoms, simplifying at the same time the data analysis. On the other hand, the (often overlooked) exploration of the averaging time dependent character of MSD is crucial for unambiguous interpretation and can provide a wealth of information on micro- and nanoscale atomic motion in proteins. General significance By properly exploiting the broad range capabilities of (quasi)elastic neutron scattering techniques to deliver time dependent characterization of atomic displacements, they offer a sensitive, direct and simple to interpret approach to exploration of the functional activity of hydrogen atoms in proteins. Partial deuteration can add most valuable selectivity by groups of hydrogen atoms. “This article is part of a Special Issue entitled “Science for Life” Guest Editor: Dr. Austen Angell, Dr. Salvatore Magazù and Dr. Federica Migliardo”.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Elastic incoherent scattering, Lamb-Mossbauer factor, Mean Square Displacement, Neutron scattering, Resolution elastic neutron scattering
in
Biochimica et Biophysica Acta - General Subjects
volume
1861
issue
1
pages
9 pages
publisher
Elsevier
external identifiers
  • scopus:84995609192
  • wos:000390745100002
ISSN
0304-4165
DOI
10.1016/j.bbagen.2016.07.030
language
English
LU publication?
yes
id
2698cdee-1f1e-4569-80f9-f5f9a9e8f96b
date added to LUP
2017-03-24 11:19:11
date last changed
2017-09-18 11:34:06
@article{2698cdee-1f1e-4569-80f9-f5f9a9e8f96b,
  abstract     = {<p>Background Elastic and quasielastic neutron scattering studies proved to be efficient probes of the atomic mean square displacement (MSD), a fundamental parameter for the characterization of the motion of individual atoms in proteins and its evolution with temperature and compositional environment. Scope of review We present a technical overview of the different types of experimental situations and the information quasi-elastic neutron scattering approaches can make available. In particular, MSD can crucially depend on the time scale over which the averaging (building of the “mean”) takes place, being defined by the instrumental resolution. Due to their high neutron scattering cross section, hydrogen atoms can be particularly sensitively observed with little interference by the other atoms in the sample. A few examples, including new data, are presented for illustration. Major conclusions The incoherent character of neutron scattering on hydrogen atoms restricts the information obtained to the self-correlations in the motion of individual atoms, simplifying at the same time the data analysis. On the other hand, the (often overlooked) exploration of the averaging time dependent character of MSD is crucial for unambiguous interpretation and can provide a wealth of information on micro- and nanoscale atomic motion in proteins. General significance By properly exploiting the broad range capabilities of (quasi)elastic neutron scattering techniques to deliver time dependent characterization of atomic displacements, they offer a sensitive, direct and simple to interpret approach to exploration of the functional activity of hydrogen atoms in proteins. Partial deuteration can add most valuable selectivity by groups of hydrogen atoms. “This article is part of a Special Issue entitled “Science for Life” Guest Editor: Dr. Austen Angell, Dr. Salvatore Magazù and Dr. Federica Migliardo”.</p>},
  author       = {Magazù, S. and Mezei, F. and Falus, Peter and Farago, Bela and Mamontov, E. and Russina, M. and Migliardo, Federica},
  issn         = {0304-4165},
  keyword      = {Elastic incoherent scattering,Lamb-Mossbauer factor,Mean Square Displacement,Neutron scattering,Resolution elastic neutron scattering},
  language     = {eng},
  month        = {01},
  number       = {1},
  pages        = {3504--3512},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - General Subjects},
  title        = {Protein dynamics as seen by (quasi) elastic neutron scattering},
  url          = {http://dx.doi.org/10.1016/j.bbagen.2016.07.030},
  volume       = {1861},
  year         = {2017},
}