Literature DB >> 16957314

Infrared temperature-jump study of the folding dynamics of alpha-helices and beta-hairpins.

Feng Gai1, Deguo Du, Yao Xu.   

Abstract

The laser-induced temperature-jump (T-jump) technique in conjunction with infrared spectroscopy provides a versatile means to study the early events in protein folding. Compared with the commonly used stopped-flow kinetic methods, the T-jump initiation technique offers a faster time resolution. It allows the study of protein folding processes occurring on the nanosecond-to-microsecond time-scales. In addition, infrared spectroscopy is a powerful tool for characterizing backbone conformation and dynamics. In this chapter, we mainly discuss the application of this technique to the study of the helix-coil transition dynamics and the mechanism of beta-hairpin formation.

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Year:  2007        PMID: 16957314     DOI: 10.1385/1-59745-189-4:1

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  4 in total

1.  The effect of charge-charge interactions on the kinetics of alpha-helix formation.

Authors:  Deguo Du; Michelle R Bunagan; Feng Gai
Journal:  Biophys J       Date:  2007-08-17       Impact factor: 4.033

2.  Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.

Authors:  Takuya Mizukami; Ming Xu; Ruzaliya Fazlieva; Valentina E Bychkova; Heinrich Roder
Journal:  J Phys Chem B       Date:  2018-08-31       Impact factor: 2.991

3.  Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.

Authors:  Yao Xu; Deguo Du; Rolando Oyola
Journal:  J Phys Chem B       Date:  2011-12-02       Impact factor: 2.991

4.  Advances in turbulent mixing techniques to study microsecond protein folding reactions.

Authors:  Sagar V Kathuria; Alexander Chan; Rita Graceffa; R Paul Nobrega; C Robert Matthews; Thomas C Irving; Blair Perot; Osman Bilsel
Journal:  Biopolymers       Date:  2013-11       Impact factor: 2.505

  4 in total

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