Molten globules
نویسنده
چکیده
When were they discovered? As early as the 1960s, there was evidence that under certain conditions protein molecules might have properties intermediate between the rigid native and fully unfolded states. The concept of such a protein as an intermediate in protein folding was suggested by the late Oleg Ptitsyn in the 1970s. A compact, partly folded protein was first observed experimentally in the early 1980s and the term molten globule was coined in 1983.
منابع مشابه
Illuminating the Off-Pathway Nature of the Molten Globule Folding Intermediate of an α-β Parallel Protein
Partially folded protein species transiently form during folding of most proteins. Often, these species are molten globules, which may be on- or off-pathway to the native state. Molten globules are ensembles of interconverting protein conformers that have a substantial amount of secondary structure, but lack virtually all tertiary side-chain packing characteristics of natively folded proteins. ...
متن کاملA view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering.
In order to understand the changes in protein dynamics that occur in the final stages of protein folding, we have used neutron scattering to probe the differences between a protein in its folded state and the molten globule states. The internal dynamics of bovine alpha-lactalbumin (BLA) and its molten globules (MBLA) have been examined using incoherent, quasielastic neutron scattering (IQNS). T...
متن کاملUsing nuclear magnetic resonance spectroscopy to study molten globule states of proteins.
Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for the study of the structure, dynamics, and folding of proteins in solution. It is particularly powerful when applied to dynamic or flexible systems, such as partially folded molten globule states of proteins, which are not usually amenable to X-ray crystallography. In this article, NMR methods suitable for the detailed cha...
متن کاملConformational selection in the molten globule state of the nuclear coactivator binding domain of CBP.
Native molten globules are the most folded kind of intrinsically disordered proteins. Little is known about the mechanism by which native molten globules bind to their cognate ligands to form fully folded complexes. The nuclear coactivator binding domain (NCBD) of CREB binding protein is particularly interesting in this respect as structural studies of its complexes have shown that NCBD folds i...
متن کاملRibosylation Rapidly Induces α-Synuclein to Form Highly Cytotoxic Molten Globules of Advanced Glycation End Products
BACKGROUND Alpha synuclein (alpha-Syn) is the main component of Lewy bodies which are associated with several neurodegenerative diseases such as Parkinson's disease. While the glycation with D-glucose that results in alpha-Syn misfold and aggregation has been studied, the effects of glycation with D-ribose on alpha-Syn have not been investigated. METHODOLOGY/PRINCIPAL FINDINGS Here, we show t...
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ورودعنوان ژورنال:
- Current Biology
دوره 9 شماره
صفحات -
تاریخ انتشار 1999