Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR
نویسندگان
چکیده
منابع مشابه
Dissecting intrinsic chaperonin activity.
It has long been known that the linear sequence of amino acids along the polypeptide chains contains all the necessary information required to determine the correct three-dimensional structure of a protein (1). Indeed, a large number of proteins have been shown to refold spontaneously in vitro from an unfolded denatured state to the native folded state (2–6). Other proteins, often large ones, h...
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 کاملDirect NMR observation of a substrate protein bound to the chaperonin GroEL.
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well characterized. In contrast, very little is known about the nonnative states of the substrate polypeptide acted on by the chaperonin machinery. In this study, we investigated the substrate protein human dihydrofolate reductase (hDHFR) while bound to GroEL or to a single-ring a...
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...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2015
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1510083112