In the present research project, an extensive NMR analysis has been carried out on four different biomolecules to clarify the structure/dynamics-function paradigm. NMR data have been integrated with structural and dynamical information provided by other biophysical and computational techniques such as SAXS and metadynamics to better characterize the structural and dynamical features of the investigated biomolecules in solution. NMR has thus been used i) for the identification of a new DNA structural folding, ii) for the speculation of the mechanism of catalysis of an enzyme, highlighting the most probable conformations in solution, iii) to underline the functional states of proteins in solution, and iv) to shed light on the mechanism of signal transduction of the Receptor for Advanced Glycation Endproducts.

Mechanistic, structural and dynamic characterization of biomolecules: from DNA to membrane proteins / Linda Cerofolini. - (2013).

Mechanistic, structural and dynamic characterization of biomolecules: from DNA to membrane proteins

CEROFOLINI, LINDA
2013

Abstract

In the present research project, an extensive NMR analysis has been carried out on four different biomolecules to clarify the structure/dynamics-function paradigm. NMR data have been integrated with structural and dynamical information provided by other biophysical and computational techniques such as SAXS and metadynamics to better characterize the structural and dynamical features of the investigated biomolecules in solution. NMR has thus been used i) for the identification of a new DNA structural folding, ii) for the speculation of the mechanism of catalysis of an enzyme, highlighting the most probable conformations in solution, iii) to underline the functional states of proteins in solution, and iv) to shed light on the mechanism of signal transduction of the Receptor for Advanced Glycation Endproducts.
2013
Claudio Luchinat
ITALIA
Linda Cerofolini
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/823331
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