منابع مشابه
Protein NMR spectroscopy
Nuclear magnetic resonance (NMR) spectroscopy uses the magnetic spin properties of atomic nuclei within a molecule to identify atoms that are close together in space (either because they are bonded together or because folds of a protein chain bring them together). This information is used to derive a three-dimensional model of a protein in solution (a ‘solution structure’). Only certain isotope...
متن کاملMillisecond 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 کاملProtein complexes studied by NMR spectroscopy.
Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point where almost any type of complex involving proteins of reasonable size may be studied in a straightforward way. A variety of isotope editing a...
متن کاملThe structural analysis of protein-protein interactions by NMR spectroscopy.
A comprehensive understanding of protein-protein interactions is an important next step in our quest to understand how the information contained in a genome is put into action. Although a number of experimental techniques can report on the existence of a protein- protein interaction, very few can provide detailed structural information. NMR spectroscopy is one of these, and in recent years seve...
متن کاملMapping protein-protein interactions in solution by NMR spectroscopy.
NMR is very well suited to the study of especially weak protein-protein interactions, as no crystallization is required. The available NMR methods to this end are reviewed and illustrated with applications from the recent biochemical literature: intermolecular NOEs, cross-saturation, chemical shift perturbation, dynamics and exchange perturbation, paramagnetic methods, and dipolar orientation. ...
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ژورنال
عنوان ژورنال: Current Biology
سال: 1998
ISSN: 0960-9822
DOI: 10.1016/s0960-9822(98)70214-3