منابع مشابه
Millisecond protein folding studied by NMR spectroscopy.
Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond time scale. Together with an overview of current a...
متن کاملNMR studies of protein folding
NMR spectroscopy is the method of choice for determining the structural details of unfolded and partially folded states of proteins. Here, the utility of NMR spectroscopy in characterizing such disordered states which populate protein folding pathways, is discussed. The relevance of the structural information obtained to protein folding mechanisms is examined critically. NMR spectroscopy can no...
متن کاملInitiation sites of protein folding by NMR analysis.
Detailed characterization of denatured states of proteins is necessary to understand the interactions that funnel the large number of possible conformations along fast routes for folding. Nuclear magnetic resonance experiments based on the nuclear Overhauser effect (NOE) detect hydrogen atoms close in space and provide information about local structure. Here we present an NMR procedure that det...
متن کاملElucidation of the protein folding landscape by NMR.
NMR is one of the few experimental methods that can provide detailed insights into the structure and dynamics of unfolded and partly folded states of proteins. Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding. In addition, it is now recognized that many proteins are intrinsically unstructured in their functional states, while partl...
متن کاملUnfolded proteins and protein folding studied by NMR.
Preparation of biological macromolecules in the pure state requires that cells be disrupted, releasing and mixing the contents. Only the most stable and highly structured molecules can survive in the cellular “soup”, which contains proteases and nucleases that would be tightly controlled and sequestered in a normal living cell. Thus, as long as “activity” of polypeptides had to be measured by c...
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ژورنال
عنوان ژورنال: Progress in Nuclear Magnetic Resonance Spectroscopy
سال: 2017
ISSN: 0079-6565
DOI: 10.1016/j.pnmrs.2016.10.002