Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent
نویسندگان
چکیده
منابع مشابه
Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent
Protein nanoassemblies possess unique advantage in biomedical applications such as drug delivery, biocatalysis and vaccine development. Despite recent accomplishment in atomic structure data, the underlying molecular mechanism of protein self-assembly remains elusive, where considerable heterogeneity is often involved. Here we use E. coli chaperonin GroEL, a tetradecameric protein with a molecu...
متن کاملStructure and allostery of the chaperonin GroEL.
Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding sites for nonnative polypeptides. Once bound, substrates are subjected to forceful, concerted movements that result in their ejection from the binding surface and simultaneous encapsulation inside a hydrophilic chamber that favors their foldi...
متن کاملMolecular mechanisms of chaperonin GroEL-GroES function.
The dynamics of the GroEL-GroES complex is investigated with a coarse-grained model. This model is one in which single-residue points are connected to other such points, which are nearby, by identical springs, forming a network of interactions. The nature of the most important (slowest) normal modes reveals a wide variety of motions uniquely dependent upon the central cavity of the structure, i...
متن کاملPutting handcuffs on the chaperonin GroEL.
Oligomeric, ring-shaped nano-machines that are fueled by ATP are ubiquitous in all three kingdoms of life and are involved in a wide range of processes that include, for example, protein folding, protein degradation, DNA and RNA remodeling, and protein insertion into membranes (for review, see ref. 1). These assemblies are true machines because they carry out work by undergoing movements that a...
متن کاملOxidized GroEL can function as a chaperonin.
Here, we report on the facilitated reactivation (85%) of oxidatively inactivated rhodanese by an oxidized form of the molecular chaperone GroEL (ox-GroEL). Reactivation by ox-GroEL required a reductant, and the enzyme substrate, sodium thiosulfate. Also, we found that ox-GroEL formed a complex with oxidatively inactivated rhodanese as shown by differential centrifugation and fluorescence spectr...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2014
ISSN: 2045-2322
DOI: 10.1038/srep05614