Unknown

Dataset Information

0

Propagating conformational changes over long (and short) distances in proteins.


ABSTRACT: The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.

SUBMITTER: Yu EW 

PROVIDER: S-EPMC55484 | BioStudies | 2001-01-01

REPOSITORIES: biostudies

Similar Datasets

2015-01-01 | S-EPMC4675818 | BioStudies
2009-01-01 | S-EPMC2695681 | BioStudies
2012-01-01 | S-EPMC3285237 | BioStudies
1000-01-01 | S-EPMC4522757 | BioStudies
2019-01-01 | S-EPMC6588728 | BioStudies
2020-01-01 | S-EPMC7380322 | BioStudies
2005-01-01 | S-EPMC555489 | BioStudies
2003-01-01 | S-EPMC154299 | BioStudies
2012-01-01 | S-EPMC3330084 | BioStudies
2013-01-01 | S-EPMC4111737 | BioStudies