Proteins conformational mobility

Protein stability is just the difference in free energy between the correctly folded structure of a protein and the unfolded, denatured form. In the denatured form, the protein is unfolded, side chains and the peptide backbone are exposed to water, and the protein is conformationally mobile (moving around between a lot of different, random structures). The more stable the protein, the larger the free energy difference between the unfolded form and the native structure. 

The properties of polypeptides and proteins are determined to a large extent by the chemistry of the side chain groups, which may be summarized briefly as follows. Glycine in a peptide permits a maximum of conformational mobility. The nine relatively nonpolar amino acids-alanine, valine, leucine, isoleucine, proline, methionine, phenylalanine, tyrosine, and tryptophan-serve as building blocks of characteristic shape. Tyrosine and tryptophan also participate in hydrogen bonding and in aromatic aromatic interactions within proteins. 

Wu, S. L., Figueroa, A., and Karger, B. L. (1986). Protein conformational effects in hydrophobic interaction chromatography. Retention characterization and the role of mobile phase additives and stationary phase hydrophobicity. J. Chromatogr. 371, 3-27. 

The first experimental evidences that electron transfer from QA to P+ and from QA to Qb in reaction centers are controlled by the protein conformational dynamics, was obtained in the late 1970 s (Berg 1978a,b Likhtenshtein et al., 1979 a, b) This conclusion was confirmed in subsequent experimental studies in which molecular dynamics of RC and the photsynthetic membrane were determined with a whole set of physical labels. (Kotelnikov et al., 1983, Kochetkov et al., 1984 Parak et al., 1983). It was shown that the electron transfer from reduced primary acceptor QA to secondary acceptor Qb takes place only under conditions in which the labels record the mobility of the protein moiety in the membrane with the correlation frequency u0 > 107 s-1 (Fig. 3.16). 

In the 1960 s and 1970 s, much indirect evidence was obtained in favour of protein intramolecular mobility, i.e. the entropy and energy specificity of enzyme catalysis (Likhtenshtein, 1966, 1976a, b, 1979, 1988 Lumry and Rajender, 1970 Lumry and Gregory, 1986). The first observations made concerned the transglobular conformational transition during substrate-protein interaction (Likhtenshtein, 1976), the reactivity of functional groups inside the protein globule, and proteolysis. 

Meserve, E. T. Direct measurement of fluorescence lifetirms. In Excited Iftates of Proteins and Nudeic Adds. Steiner, R. F., Weinryb, I. (Eds.) p. 57, New York Plenum 1971 Morawetz, H. Fluorescence studies of conformational mobility and of the mutual interpenetration of flexible chain molecules. WPAC Symposium Macromol. Qiem. Mainz. In press, communicated privately... 

---