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Nonequilibrium NMR Methods for Monitoring Protein and RNA Folding
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Kai Schlepckow
Published/Copyright:
May 3, 2011
Abstract
The review introduces to time-resolved NMR spectroscopic investigations of the kinetics of protein and RNA folding. The description of the experimental investigations is discussed in the context of possible kinetic folding pathways showing the extent of information that can be gained from the various kinetic experiments. The review introduces to four different methods to initiate folding reactions in connection with time-resolved NMR experiments and discusses examples of refolding of the model protein α-lactalbumin and of bistable RNAs.
Published Online: 2011-5-3
Published in Print: 2011-5-1
© by Oldenbourg Wissenschaftsverlag, München, Germany
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Articles in the same Issue
- Editorial
- Reactions between Cold CHx+ and Slow H and H2
- Reactions in Trifluoropropene and Trifluoropropyne Triggered by Low-Energy (0–12 eV) Electrons: From Single Bond Cleavages to Complex Unimolecular Decompositions
- Direct Access to the Dipole-Forbidden nπ∗T1 State of p-Benzoquinone by Photodetachment Photoelectron Spectroscopy
- Quantitative Study of 4He Real Gas Effects Using Supersonic Beams
- Large Amplitude Motions in Cyclopentene and 1-Butene: Quantum Chemical Insights into the Ground- and Excited State Potential Energy Surfaces
- Coherent Excitation Transfer Driven by Torsional Dynamics: a Model Hamiltonian for PPV Type Systems
- H-Bonding Cooperativity Effects in Amyloids: Quantum Mechanical and Molecular Mechanics Study
- Ultrafast Charge Separation at the CdSe Quantum Dot/Methylviologen Interface: Dependence on Electron Acceptor Concentration
- Circular Dichroism in Ion Yields in Multiphoton Ionization of (R)-Propylene Oxide Employing Femtosecond Laser Pulses
- The Interaction of the Dipeptide Carnosine With Alkali Metal Ions Studied by Ion Trap Mass Spectrometry
- Nonequilibrium NMR Methods for Monitoring Protein and RNA Folding
