Intramolecular dynamics and conformational transition in proteins studied by biophysical labelling methods. Common and specific features of proteins from thermophylic micro-organisms.
A general survey is carried out on the theoretical grounds for methods of spin, luminescence and Mössbauer labels, as well as their application in the study of protein intramolecular dynamics. When combined, these methods allow the protein dynamics to be investigated within a wide range of correlation times (tau c = 10(2) - 10(-10) s) and amplitudes. The purposeful application of the methods to various proteins at different temperatures (30-330 K), water content, substrate addition, etc., revealed a number of dynamical processes and conformational transitions in proteins. The experiments indicated correlations between the local segmental mobility of protein globules in a nanosecond temporal scale and biochemical reactions, such as long-distance electron transfer, hydrolysis and photoreactions. The biophysical labelling methods results were analysed together with the data on dynamics obtained using complementary physico-chemical methods and theoretical calculations. Special emphasis is given to recent results on proteins from thermophylic micro-organisms. The mechanisms of protein intramolecular dynamics and their role in the stability and functions of proteins and enzymes are discussed.
Likhtenshtein
G I
GI
Department of Chemistry, Ben Gurion University of Negev, Beer-Sheva, Israel. gertz@bgumail.bgu.ac.il
Febbraio
F
F
Nucci
R
R
D002627:Chemistry, Physical / Q000379:methods*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*; D013113:Spin Labels; D013696:Temperature; D014961:X-Ray Diffraction / Q000379:methods
D009211:Myoglobin; D012709:Serum Albumin; D013113:Spin Labels; D009113:Muramidase