A model-free analysis of the 1H nuclear magnetic relaxation dispersion (NMRD) profiles of 14 proteins in aqueous solution was performed to reproduce the experimental dispersions, that are stretched with respect to Lorentzians. The analysis, according to a recently proposed approach, shows a good correlation of all physically meaningful parameters with the molecular weight of the proteins, spanning the range from 6500 to 480 000, and, in particular, of the average correlation time with the Stokes–Einstein estimate of the rotational correlation time.

H-1 NMRD profiles of diamagnetic proteins: a model-free analysis / I. Bertini; M. Fragai; C. Luchinat; G. Parigi. - In: MAGNETIC RESONANCE IN CHEMISTRY. - ISSN 0749-1581. - STAMPA. - 38:(2000), pp. 543-550. [10.1002/1097-458X(200007)38:7<543::AID-MRC722>3.0.CO;2-#]

H-1 NMRD profiles of diamagnetic proteins: a model-free analysis

BERTINI, IVANO;FRAGAI, MARCO;LUCHINAT, CLAUDIO;PARIGI, GIACOMO
2000

Abstract

A model-free analysis of the 1H nuclear magnetic relaxation dispersion (NMRD) profiles of 14 proteins in aqueous solution was performed to reproduce the experimental dispersions, that are stretched with respect to Lorentzians. The analysis, according to a recently proposed approach, shows a good correlation of all physically meaningful parameters with the molecular weight of the proteins, spanning the range from 6500 to 480 000, and, in particular, of the average correlation time with the Stokes–Einstein estimate of the rotational correlation time.
38
543
550
I. Bertini; M. Fragai; C. Luchinat; G. Parigi
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2158/354813
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