[Fluctuational intramolecular mobility of proteins using physical labels].
An analysis of spin,- fluorescence, triplet- and Mössbauer labeling techniques is given as well as the method of radical pair recombination for investigation of globular proteins molecular dynamics in the temperature range of 50-300 K and correlation time tau c = 10(-2) - 10(11) s-1. Based on experimental evidence and literature data a conclusion is drawn on the existence of protein microheterogeneity at negative temperatures. A dynamic model of a globular protein is proposed. It is supposed to be a system of tightly-packed polypeptide proteins blocks connected by hinge-like linkage with a few degrees of freedom. The system is sunk in viscous amorphous medium composed of superficial protein groups and bound water molecules. The correlation between the protein molecular dynamics and enzymes activities is discussed.
D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D008433:Mathematics; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins; D013050:Spectrometry, Fluorescence / Q000379:methods; D013057:Spectrum Analysis / Q000379:methods; D013696:Temperature
D011506:Proteins
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