caa a22 4500 606243011 CHVBK 20210128101321.0 cr unu---uuuuu 210128e20150601xx s 000 0 eng 10.1007/s12551-015-0166-6 doi (NATIONALLICENCE)springer-10.1007/s12551-015-0166-6 Relaxation dispersion NMR spectroscopy for the study of protein allostery [Elektronische Daten] [Patrick Farber, Anthony Mittermaier] Allosteric transmission of information between distant sites in biological macromolecules often involves collective transitions between active and inactive conformations. Nuclear magnetic resonance (NMR) spectroscopy can yield detailed information on these dynamics. In particular, relaxation dispersion techniques provide structural, dynamic, and mechanistic information on conformational transitions occurring on the millisecond to microsecond timescales. In this review, we provide an overview of the theory and analysis of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiments and briefly describe their application to the study of allosteric dynamics in the homeodomain from the PBX transcription factor (PBX-HD). CPMG NMR data show that local folding (helix/coil) transitions in one part of PBX-HD help to communicate information between two distant binding sites. Furthermore, the combination of CPMG and other spin relaxation data show that this region can also undergo local misfolding, reminiscent of conformational ensemble models of allostery. International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg, 2015 Allostery nationallicence Nuclear magnetic resonance nationallicence Carr-Purcell-Meiboom-Gill nationallicence PBX homeodomain nationallicence Three-state exchange nationallicence Misfolding nationallicence Farber Patrick Molecular Structure and Function, Hospital for Sick Children, Toronto, ON, Canada aut Mittermaier Anthony Department of Chemistry, McGill University, 801 Sherbrooke St. W. room 322, H3A 0B8, Montreal, Quebec, Canada aut Biophysical Reviews Springer Berlin Heidelberg 7/2(2015-06-01), 191-200 1867-2450 7:2<191 2015 7 12551 https://doi.org/10.1007/s12551-015-0166-6 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s12551-015-0166-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Farber Patrick Molecular Structure and Function, Hospital for Sick Children, Toronto, ON, Canada aut NATIONALLICENCE 700 1- Mittermaier Anthony Department of Chemistry, McGill University, 801 Sherbrooke St. W. room 322, H3A 0B8, Montreal, Quebec, Canada aut NATIONALLICENCE 773 0- Biophysical Reviews Springer Berlin Heidelberg 7/2(2015-06-01), 191-200 1867-2450 7:2<191 2015 7 12551