Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements

Autor: Sarah, Leeb, Jens, Danielsson
Rok vydání: 2020
Předmět:
Zdroj: Methods in molecular biology (Clifton, N.J.). 2141
ISSN: 1940-6029
Popis: In the disordered state, a protein exhibits a high degree of structural freedom, in both space and time. For an ensemble of disordered or unfolded proteins, this means that the ensemble comprises a high diversity of structures, ranging from compact collapsed states to fully extended polypeptide chains. In addition, each chain is highly dynamic and undergoes conformational changes and local dynamics on both fast and slow timescales. The size properties of disordered proteins are thus best described as ensemble averages. A straightforward measure of the size is the hydrodynamic radius, R
Databáze: OpenAIRE