Dynamic Coupling and Allosteric Behavior in a Nonallosteric Protein†
نویسندگان
چکیده
منابع مشابه
Dynamic coupling and allosteric behavior in a nonallosteric protein.
Long-range intraprotein interactions give rise to many important protein behaviors. Understanding how energy is transduced through protein structures to either transmit a signal or elicit conformational changes is therefore a current challenge in structural biology. In an effort to understand such linkages, multiple V --> A mutations were made in the small globular protein eglin c. The physical...
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Background: The bacterial adhesin FimH is allosterically regulated. Results: Mutations designed to control the allosteric state of the protein created low or high affinity variants as predicted. Conclusion: Three regulatory regions are strongly coupled together, while the active site is more weakly coupled to those regions. Significance: Allosteric regulation can be used to develop antiadhesive...
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Escherichia coli chaperonin, GroEL, helps proteins fold under nonpermissive conditions. During the reaction cycle, GroEL undergoes allosteric transitions in response to binding of a substrate protein (SP), ATP, and the cochaperonin GroES. Using coarse-grained representations of the GroEL and GroES structures, we explore the link between allosteric transitions and the folding of a model SP, a de...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 2006
ISSN: 0006-2960,1520-4995
DOI: 10.1021/bi060652l