The presence of heterogeneity in the interdomain arrangement of several biomolecules is required for their function. Here we present a method to obtain crucial clues to distinguish between different kinds of protein conformational distributions based on experimental NMR data. The method explores subregions of the conformational space and provides both upper and lower bounds of probability for the system to be in each subregion.
Exploring Regions of Conformational Space Occupied by Two-Domain Proteins / Witold Andralojc;Claudio Luchinat;Giacomo Parigi;Enrico Ravera. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - STAMPA. - 118:(2014), pp. 10576-10587. [10.1021/jp504820w]
Exploring Regions of Conformational Space Occupied by Two-Domain Proteins
ANDRALOJC, WITOLD JACEK;LUCHINAT, CLAUDIO;PARIGI, GIACOMO;RAVERA, ENRICO
2014
Abstract
The presence of heterogeneity in the interdomain arrangement of several biomolecules is required for their function. Here we present a method to obtain crucial clues to distinguish between different kinds of protein conformational distributions based on experimental NMR data. The method explores subregions of the conformational space and provides both upper and lower bounds of probability for the system to be in each subregion.
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