caa a22 4500 606243003 CHVBK 20210128101321.0 cr unu---uuuuu 210128e20150601xx s 000 0 eng 10.1007/s12551-015-0172-8 doi (NATIONALLICENCE)springer-10.1007/s12551-015-0172-8 The role of slow and fast protein motions in allosteric interactions [Elektronische Daten] [Shiou-Ru Tzeng, Charalampos Kalodimos] Allostery is fundamentally thermodynamic in nature. Long-range communication in proteins may be mediated not only by changes in the mean conformation with enthalpic contribution but also by changes in dynamic fluctuations with entropic contribution. The important role of protein motions in mediating allosteric interactions has been established by NMR spectroscopy. By using CAP as a model system, we have shown how changes in protein structure and internal dynamics can allosterically regulate protein function and activity. The results indicate that changes in conformational entropy can give rise to binding enhancement, binding inhibition, or have no effect in the expected affinity, depending on the magnitude and sign of enthalpy-entropy compensation. Moreover, allosteric interactions can be regulated by the modulation a low-populated conformation states that serve as on-pathway intermediates for ligand binding. Taken together, the interplay between fast internal motions, which are intimately related to conformational entropy, and slow internal motions, which are related to poorly populated conformational states, can regulate protein activity in a way that cannot be predicted on the basis of the protein's ground-state structure. International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg, 2015 NMR spectroscopy nationallicence Catabolite activator protein nationallicence Cyclic nucleotide-binding nationallicence Tzeng Shiou-Ru Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, 100, Taipei, Taiwan aut Kalodimos Charalampos Center for Integrative Proteomics Research & Department of Chemistry & Chemical Biology, Rutgers University, Piscataway, New Jersey, USA aut Biophysical Reviews Springer Berlin Heidelberg 7/2(2015-06-01), 251-255 1867-2450 7:2<251 2015 7 12551 https://doi.org/10.1007/s12551-015-0172-8 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s12551-015-0172-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tzeng Shiou-Ru Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, 100, Taipei, Taiwan aut NATIONALLICENCE 700 1- Kalodimos Charalampos Center for Integrative Proteomics Research & Department of Chemistry & Chemical Biology, Rutgers University, Piscataway, New Jersey, USA aut NATIONALLICENCE 773 0- Biophysical Reviews Springer Berlin Heidelberg 7/2(2015-06-01), 251-255 1867-2450 7:2<251 2015 7 12551