Functional Unfolding in E. coli Adenylate Kinase
نویسندگان
چکیده
منابع مشابه
Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins.
Elucidating the complex interplay between protein structure and dynamics is a prerequisite to an understanding of both function and adaptation in proteins. Unfortunately, it has been difficult to experimentally decouple these effects because it is challenging to rationally design mutations that will either affect the structure but not the dynamics, or that will affect the dynamics but not the s...
متن کاملProtein folding pathways of adenylate kinase from E. coli: hydrostatic pressure and stopped-flow studies.
Adenylate kinase (AKe) from E. coli is a small, single-chain, monomeric enzyme with no tryptophan and a single cysteine residue. We have constructed six single-Trp mutants of AKe to facilitate optical studies of these proteins and to specifically examine the interrelationship between their structure, function, dynamics, and folding reactions. In this study, the effects of hydrostatic pressure o...
متن کاملE VALUATION OF ADENYLATE CYCLASE ACTIVITY IN MITRAL VALVE PROLAPSE
The term mitral valve prolapse (MVP) is used for a particular subset of patients with hyperadrenergic dysautonomia. It occurs when part of a leaflet or both leaflets of the mitral valve extend above the plane of the atrioventricular junction during ventricular systole. The adenylate cyclase activity in MVP dys-autonomia was studied by extraction of enzyme from the erythrocytes from 62 norma...
متن کاملCircular dichroism investigation of Escherichia coli adenylate kinase.
We examined by circular dichroism (CD) spectroscopy in far- and near-ultraviolet three different molecular forms of Escherichia coli adenylate kinase: the wild type protein, the enzyme carboxymethylated at a single cysteine residue (Cys-77), and the thermosensitive adenylate kinase. The thermosensitive enzyme differs from the wild type protein in that a serine is substituted for a proline resid...
متن کاملInorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli.
Polyphosphate kinase (PPK), responsible for the processive synthesis of inorganic polyphosphate (polyP) from ATP in Escherichia coli, can transfer in reverse the terminal phosphate residue of polyP to ADP to yield ATP. PolyP also serves as a donor in a polyP:AMP phosphotransferase (PAP) activity observed in extracts of Acinetobacter johnsonii and Myxococcus xanthus. We have found that overexpre...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2015
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2014.11.190