Literature DB >> 3040467

Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism.

K Kuwajima, H Yamaya, S Miwa, S Sugai, T Nagamura.   

Abstract

Kinetic refolding reactions of ferricytochrome c and beta-lactoglobulin have been studied by stopped-flow circular dichroism by monitoring rapid ellipticity changes of peptide backbone and side-chain chromophores. In both proteins, a transient intermediate accumulates within the dead time of stopped-flow mixing (18 ms), and the intermediate has an appreciable amount of secondary structure but possesses an unfolded tertiary structure. It is suggested that the rapid formation of a secondary structure framework in protein folding is a common property observed in a variety of globular proteins.

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Year:  1987        PMID： 3040467     DOI： 10.1016/0014-5793(87)80363-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  39 in total

1.  The alpha-helix folds on the millisecond time scale.

Authors:  D T Clarke; A J Doig; B J Stapley; G R Jones
Journal:  Proc Natl Acad Sci U S A       Date:  1999-06-22       Impact factor: 11.205

2.  Stepwise helix formation and chain compaction during protein folding.

Authors:  Heinrich Roder
Journal:  Proc Natl Acad Sci U S A       Date:  2004-02-09       Impact factor: 11.205

3.  Formation of amyloid fibrils from fully reduced hen egg white lysozyme.

Authors:  Aoneng Cao; Daoying Hu; Luhua Lai
Journal:  Protein Sci       Date:  2004-01-10       Impact factor: 6.725

4.  Reversible and fast association equilibria of a molecular chaperone, gp57A, of bacteriophage T4.

Authors:  Said A Ali; Noriyuki Iwabuchi; Takuro Matsui; Ken Hirota; Shun-Ichi Kidokoro; Munehito Arai; Kunihiro Kuwajima; Peter Schuck; Fumio Arisaka
Journal:  Biophys J       Date:  2003-10       Impact factor: 4.033

Review 5.  Protein folding.

Authors:  T E Creighton
Journal:  Biochem J       Date:  1990-08-15       Impact factor: 3.857

6.  The role of secondary structure in protein structure selection.

Authors:  Yong-Yun Ji; You-Quan Li
Journal:  Eur Phys J E Soft Matter       Date:  2010-05-25       Impact factor: 1.890

Review 7.  Molten globule intermediates and protein folding.

Authors:  H Christensen; R H Pain
Journal:  Eur Biophys J       Date:  1991       Impact factor: 1.733

8.  Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study.

Authors:  C Bhattacharjee; S Saha; A Biswas; M Kundu; L Ghosh; K P Das
Journal:  Protein J       Date:  2005-01       Impact factor: 2.371

Review 9.  Early events in protein folding explored by rapid mixing methods.

Authors:  Heinrich Roder; Kosuke Maki; Hong Cheng
Journal:  Chem Rev       Date:  2006-05       Impact factor: 60.622

10.  Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway.

Authors:  Jason Cellitti; Rachel Bernstein; Susan Marqusee
Journal:  Protein Sci       Date:  2007-03-30       Impact factor: 6.725
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