We have shown that data from direct protein 1H relaxation dispersion yield information on: 1) the lack of rigidity through S2, which is directly related to the range of folded states of the protein (from fully folded to the extreme state of complete unfolding) and 2) protein aggregation through a safe estimate of τR.
NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz / I. Bertini; Y. K. Gupta; C. Luchinat; G. Parigi; C. Schlorb; H. Schwalbe. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 44:(2005), pp. 2223-2225. [10.1002/anie.200462344]
NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHz
BERTINI, IVANO;LUCHINAT, CLAUDIO;PARIGI, GIACOMO;
2005
Abstract
We have shown that data from direct protein 1H relaxation dispersion yield information on: 1) the lack of rigidity through S2, which is directly related to the range of folded states of the protein (from fully folded to the extreme state of complete unfolding) and 2) protein aggregation through a safe estimate of τR.
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