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Relaxation and Disorder in Proteins

  • Chapter
Disorder Effects on Relaxational Processes

Abstract

It has become increasingly clear that proteins share essential characteristics with glasses, spin glasses, and other complex systems [1–5]. This comparison may initially seem contradictory: Proteins are macromolecules with well-defined X-ray structures [6] while glasses are frozen liquids [7, 8]. This view ignores the fact that proteins share one fundamental property with glasses [9] and other complex systems such as spin glasses [10, 11], molecular evolution [12, 13], and neural nets [14]: Proteins have a rugged energy landscape with a large number of energy minima (valleys) separated by energy maxima and saddle points [3, 4, 15, 16]. The energy valleys correspond to slightly different structures in a protein [17] or a structural glass [18] and are called conformational substates (CS) [19]. The evidence for conformational substates in proteins coming from low-temperature, ligand-protein binding studies as well as temperature-dependent Mossbauer and X-ray diffraction studies is summarized in [19].

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Abbreviations

CS:

conformational substate

MEM:

maximum entropy method

RSMR:

Rayleigh scattering of Mossbauer radiation

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Authors
  1. H. Frauenfelder
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  2. G. U. Nienhaus
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  3. R. D. Young
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Editor information

Editors and Affiliations

  1. Max-Planck-Institut für Polymerforschung, Ackermannweg 10, 55128, Mainz, Germany

    Ranko Richert

  2. Theoretische Polymerphysik Albert-Ludwigs-Universität, Rheinstr 12, 79104, Freiburg, Germany

    Alexander Blumen

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© 1994 Springer-Verlag Berlin Heidelberg

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Frauenfelder, H., Nienhaus, G.U., Young, R.D. (1994). Relaxation and Disorder in Proteins. In: Richert, R., Blumen, A. (eds) Disorder Effects on Relaxational Processes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78576-4_21

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  • DOI: https://doi.org/10.1007/978-3-642-78576-4_21

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-78578-8

  • Online ISBN: 978-3-642-78576-4

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