Literature DB >> 10494843

Elementary steps in protein folding.

O Bieri1, T Kiefhaber.   

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 alpha-helices, beta-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.

Mesh:

Year:  1999        PMID: 10494843     DOI: 10.1515/BC.1999.114

Source DB:  PubMed          Journal:  Biol Chem        ISSN: 1431-6730            Impact factor:   3.915


  4 in total

1.  Effects of Mutations on the Reconfiguration Rate of α-Synuclein.

Authors:  Srabasti Acharya; Shreya Saha; Basir Ahmad; Lisa J Lapidus
Journal:  J Phys Chem B       Date:  2015-12-04       Impact factor: 2.991

2.  Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility.

Authors:  J Wachtveitl; S Spörlein; H Satzger; B Fonrobert; C Renner; R Behrendt; D Oesterhelt; L Moroder; W Zinth
Journal:  Biophys J       Date:  2004-04       Impact factor: 4.033

3.  Kinetics of chain motions within a protein-folding intermediate.

Authors:  Hannes Neuweiler; Wiktor Banachewicz; Alan R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  2010-12-06       Impact factor: 11.205

4.  Enhanced Sensitivity to Local Dynamics in Peptides by Use of Temperature-Jump IR Spectroscopy and Isotope Labeling.

Authors:  David Scheerer; Heng Chi; Dan McElheny; Timothy A Keiderling; Karin Hauser
Journal:  Chemistry       Date:  2020-02-04       Impact factor: 5.236

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.