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Fast events in protein folding: the time evolution of primary processes

Article Abstract:

Most experimental studies on protein folding dynamics have been limited to timescales of 1 ms or more. It is clear that many phenomena necessary for folding of proteins occur in a much shorter time than that. Formation of tertiary and secondary structures can take place on microsecond and nanosecond timescales, respectively. The fast events are required and dominate at times, but with only a few exceptions the study of these events experimentally has been possible only lately. New approaches can start and monitor the fast events with temporal resolution going down to picoseconds. Some important results for folding of some globular proteins and polypeptide models are now available.

Author: Dyer, R. Brian, Woodruff, William H., Callender, Robert H., Gilmanshin, Rudolf
Publisher: Annual Reviews, Inc.
Publication Name: Annual Review of Physical Chemistry
Subject: Chemistry
ISSN: 0066-426X
Year: 1998
Measurement, Observations, Structure-activity relationships (Biochemistry), Chemical reaction, Rate of, Chemical kinetics, Infrared spectra

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Early events in RNA folding

Article Abstract:

The early events in RNA folding in Tetrahymena ribozyme constitute collapse of RNA molecules caused by counterion-condensation and occur on microsecond time scales. Large RNA molecules follow the kinetic partitioning mechanism, in which a small fraction folds rapidly to the native state with the remaining kinetically trapped in a low-energy non-native state.

Author: Thirumalai, D., Lee, Namkyung, Woodson, Sarah A., Klimov, DK
Publisher: Annual Reviews, Inc.
Publication Name: Annual Review of Physical Chemistry
Subject: Chemistry
ISSN: 0066-426X
Year: 2001
Research, Models, Physiological aspects, RNA, Nucleic acids, Catalytic RNA

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The fast protein folding problem

Article Abstract:

This article examines the fast folding events during the course of protein folding employing nuclear magnetic resonance and laser techniques. Fast protein folding reactions are illustrated with simple proteins and quantitative models.

Author: Gruebele, M.
Publisher: Annual Reviews, Inc.
Publication Name: Annual Review of Physical Chemistry
Subject: Chemistry
ISSN: 0066-426X
Year: 1999
Methods, Analysis, Nuclear magnetic resonance spectroscopy, Protein engineering, Protein structure, Raman effect, Circular dichroism

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Subjects list: United States, Usage, Proteins, Protein folding, Spectra, Protein denaturation
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