منابع مشابه
Time-resolved infrared spectroscopy of RNA folding.
We introduce time-resolved infrared spectroscopy as a powerful method to study the kinetics of RNA folding and unfolding transitions. A laser-induced temperature jump is used to initiate a perturbation in the RNA structure. A probe laser, tuned to a specific infrared absorption of the RNA, is then used to monitor the subsequent relaxation kinetics. A 10-ns pump pulse permits the investigation o...
متن کاملTime-resolved NMR methods resolving ligand-induced RNA folding at atomic resolution.
Structural transitions of RNA between alternate conformations with similar stabilities are associated with important aspects of cellular function. Few techniques presently exist that are capable of monitoring such transitions and thereby provide insight into RNA dynamics and function at atomic resolution. Riboswitches are found in the 5'-UTR of mRNA and control gene expression through structura...
متن کاملTheoretical studies of time-resolved spectroscopy of protein folding.
Recently, we have made significant improvements in the accuracy of calculations of the circular dichroism of proteins from first principles. The quality of these calculations (especially at 220 nm, a key wavelength, where the intensity of the band correlates well with the helical content of polypeptides) has given us confidence to use such calculations to analyse nanosecond molecular dynamics s...
متن کاملTime-resolved X-ray scattering and RNA folding.
Time-resolved small-angle X-ray scattering (SAXS) reports changes in the global conformation of macromolecules and is thus a valuable probe of structural transitions like RNA folding. Time-resolved SAXS has been applied to study folding of the Tetrahymena ribozyme. This chapter describes the methods that enable acquisition and analysis of time-resolved SAXS data and insights into RNA folding ga...
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...
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ژورنال
عنوان ژورنال: Biopolymers
سال: 2007
ISSN: 0006-3525,1097-0282
DOI: 10.1002/bip.20761