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Concepts and problems in protein dynamics

Fenimore, Paul W. ; Frauenfelder, Hans ; Magazu, Salvatore ; McMahon, Benjamin H. ; Mezei, Ferenc LU ; Migliardo, Federica ; Young, Robert D. and Stroe, Izabela (2013) In Chemical Physics 424. p.2-6
Abstract
The function of proteins depends crucially on conformational motions. The characteristic times of these motions extend from sub-picosecond to seconds. No single experimental tool can cover the entire time range and provide all necessary parameters for a complete understanding. Moreover, without a solid understanding of the data evaluation it is easy to misinterpret the complex phenomena. Because protein motions are truly complex, the evaluation of the data even from such well-known techniques as neutron scattering (Magazu and Migliardo, 2011 [1]) and the Mossbauer effect (Chen and Yang, 2007 [2]) can lead to erroneous concepts and conclusions. We believe that notions such as the Lamb-Mossbauer relation, the protein dynamic transition, the... (More)
The function of proteins depends crucially on conformational motions. The characteristic times of these motions extend from sub-picosecond to seconds. No single experimental tool can cover the entire time range and provide all necessary parameters for a complete understanding. Moreover, without a solid understanding of the data evaluation it is easy to misinterpret the complex phenomena. Because protein motions are truly complex, the evaluation of the data even from such well-known techniques as neutron scattering (Magazu and Migliardo, 2011 [1]) and the Mossbauer effect (Chen and Yang, 2007 [2]) can lead to erroneous concepts and conclusions. We believe that notions such as the Lamb-Mossbauer relation, the protein dynamic transition, the protein glass transition, and the dynamic crossover are misleading or misapplied. To justify this statement we first briefly describe our view of dynamic proteins and then explain why we believe that these notions should be revised or abandoned. (C) 2013 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Protein dynamics, Neutron scattering, Mossbauer spectroscopy
in
Chemical Physics
volume
424
pages
2 - 6
publisher
Elsevier
external identifiers
  • wos:000326983700002
  • scopus:84888292325
ISSN
0301-0104
DOI
10.1016/j.chemphys.2013.06.023
language
English
LU publication?
yes
id
85d82d45-4652-4a0b-b79b-1b14e5573155 (old id 4197800)
date added to LUP
2016-04-01 13:17:59
date last changed
2020-01-12 11:49:00
@article{85d82d45-4652-4a0b-b79b-1b14e5573155,
  abstract     = {The function of proteins depends crucially on conformational motions. The characteristic times of these motions extend from sub-picosecond to seconds. No single experimental tool can cover the entire time range and provide all necessary parameters for a complete understanding. Moreover, without a solid understanding of the data evaluation it is easy to misinterpret the complex phenomena. Because protein motions are truly complex, the evaluation of the data even from such well-known techniques as neutron scattering (Magazu and Migliardo, 2011 [1]) and the Mossbauer effect (Chen and Yang, 2007 [2]) can lead to erroneous concepts and conclusions. We believe that notions such as the Lamb-Mossbauer relation, the protein dynamic transition, the protein glass transition, and the dynamic crossover are misleading or misapplied. To justify this statement we first briefly describe our view of dynamic proteins and then explain why we believe that these notions should be revised or abandoned. (C) 2013 Elsevier B.V. All rights reserved.},
  author       = {Fenimore, Paul W. and Frauenfelder, Hans and Magazu, Salvatore and McMahon, Benjamin H. and Mezei, Ferenc and Migliardo, Federica and Young, Robert D. and Stroe, Izabela},
  issn         = {0301-0104},
  language     = {eng},
  pages        = {2--6},
  publisher    = {Elsevier},
  series       = {Chemical Physics},
  title        = {Concepts and problems in protein dynamics},
  url          = {http://dx.doi.org/10.1016/j.chemphys.2013.06.023},
  doi          = {10.1016/j.chemphys.2013.06.023},
  volume       = {424},
  year         = {2013},
}