Elementary Steps in Protein Folding
-
O. Bieri
Abstract
The mechanism of protein folding is under intense theoretical and experimental investigation. From stopped-flow mixing experiments we have detailed knowledge of processes slower than about 1 ms, but until recently little was known about folding and unfolding reactions on the microsecond to nanosecond time scale. The use of novel techniques allowed to explore the elementary steps in protein folding, such as intrachain diffusion and formation of α-helices, β-hairpins and loop structures. This brief review discusses the time scales of these early elementary events which are crucial for the understanding of how proteins fold.
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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- Mutant p53: Gain-of-Function Oncoproteins and Wild-Type p53 Inactivators
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- Agonist-Stimulated Pathways of Calcium Signaling in Pancreatic Acinar Cells
- Some of the Early Events Underlying Th2. Cell Maturation and Susceptibility to Leishmania major Infection in BALB/c Mice
- Universal and Unique Features of Kinesin Motors: Insights from a Comparison of Fungal and Animal Conventional Kinesins
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- Molecular Reaction Mechanisms of Proteins Monitored by Time-Resolved FTIR-Spectroscopy
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