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Protein dynamics as...
Protein dynamics as seen by (quasi) elastic neutron scattering
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- Magazù, S. (författare)
- University of Messina
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- Mezei, F. (författare)
- Lund University,Lunds universitet,European Spallation Source ESS AB,Stiftelser och övriga anknutna verksamheter,Other Institutions and Utilities,Hungarian Academy of Sciences
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- Falus, Peter (författare)
- Institut Laue Langevin
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- Farago, Bela (författare)
- Institut Laue Langevin
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- Mamontov, E. (författare)
- Oak Ridge National Laboratory
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- Russina, M. (författare)
- Helmholtz Association of German Research Centers
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- Migliardo, Federica (författare)
- University of Paris-Saclay,University of Messina
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(creator_code:org_t)
- Elsevier BV, 2017
- 2017
- Engelska 9 s.
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Ingår i: Biochimica et Biophysica Acta - General Subjects. - : Elsevier BV. - 0304-4165. ; 1861:1, s. 3504-3512
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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”.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- NATURVETENSKAP -- Fysik -- Subatomär fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences -- Subatomic Physics (hsv//eng)
Nyckelord
- Elastic incoherent scattering
- Lamb-Mossbauer factor
- Mean Square Displacement
- Neutron scattering
- Resolution elastic neutron scattering
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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