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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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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