منابع مشابه
Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.
Fits of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion profiles allow extraction of the kinetics and thermodynamics of exchange reactions that interconvert highly populated, ground state and low populated, excited state conformers. Structural information is also available in the form of chemical shift differences between the interconverting protein states. Here we present a very simple ...
متن کاملStructures of invisible, excited protein states by relaxation dispersion NMR spectroscopy.
Molecular function is often predicated on excursions between ground states and higher energy conformers that can play important roles in ligand binding, molecular recognition, enzyme catalysis, and protein folding. The tools of structural biology enable a detailed characterization of ground state structure and dynamics; however, studies of excited state conformations are more difficult because ...
متن کاملStudying "invisible" excited protein states in slow exchange with a major state conformation.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and characterize "invisible" excited protein states in slo...
متن کاملUsing relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states.
Currently the main focus of structural biology is the determination of static three-dimensional representations of biomolecules that for the most part correspond to low energy (ground state) conformations. However, it is becoming increasingly well recognized that higher energy structures often play important roles in function as well. Because these conformers are populated to only low levels an...
متن کاملReconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.
Carr-Purcell-Meiboom-Gill (CPMG) relaxation measurements employing trains of 180 degrees pulses with variable pulse spacing provide valuable information about systems undergoing millisecond-time-scale chemical exchange. Fits of the CPMG relaxation dispersion profiles yield rates of interconversion, relative populations, and absolute values of chemical shift differences between the exchanging st...
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ژورنال
عنوان ژورنال: The Scientific World JOURNAL
سال: 2002
ISSN: 1537-744X
DOI: 10.1100/tsw.2002.23