Literature DB >> 9270297

Hydrogen exchange at equilibrium: a short cut for analysing protein-folding pathways?

J Clarke1, L S Itzhaki, A R Fersht.   

Abstract

Hydrogen exchange is an attractive method for observing small populations of partly unfolded states of proteins at equilibrium. It has been suggested that these represent folding intermediates so that hydrogen exchange can offer a short cut for studying protein-folding pathways. This cannot work in theory because it is not possible to tell whether they are intermediates or side reactions. Experimental studies of barnase and chymotrypsin inhibitor 2 show that there is no obvious relationship between hydrogen exchange at equilibrium and their folding pathways.

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Year:  1997        PMID： 9270297     DOI： 10.1016/s0968-0004(97)01087-6

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN： 0968-0004            Impact factor:   13.807


  15 in total

Review 1.  The hydrogen exchange core and protein folding.

Authors:  R Li; C Woodward
Journal:  Protein Sci       Date:  1999-08       Impact factor: 6.725

2.  Partially unfolded forms and non-two-state folding of a beta-sandwich: FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.

Authors:  Xiangyang Liang; Gui-in Lee; Steven R Van Doren
Journal:  J Mol Biol       Date:  2006-09-03       Impact factor: 5.469

3.  The folding energy landscape of apoflavodoxin is rugged: hydrogen exchange reveals nonproductive misfolded intermediates.

Authors:  Yves J M Bollen; Monique B Kamphuis; Carlo P M van Mierlo
Journal:  Proc Natl Acad Sci U S A       Date:  2006-03-06       Impact factor: 11.205

4.  The extremely slow-exchanging core and acid-denatured state of green fluorescent protein.

Authors:  Jie-Rong Huang; Shang-Te Danny Hsu; John Christodoulou; Sophie E Jackson
Journal:  HFSP J       Date:  2008-09-15

5.  The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.

Authors:  Ellinor Haglund; Jesper Lind; Tommy Oman; Anders Ohman; Lena Mäler; Mikael Oliveberg
Journal:  Proc Natl Acad Sci U S A       Date:  2009-12-04       Impact factor: 11.205

6.  How internal cavities destabilize a protein.

Authors:  Mengjun Xue; Takuro Wakamoto; Camilla Kejlberg; Yuichi Yoshimura; Tania Aaquist Nielsen; Michael Wulff Risør; Kristian Wejse Sanggaard; Ryo Kitahara; Frans A A Mulder
Journal:  Proc Natl Acad Sci U S A       Date:  2019-09-30       Impact factor: 11.205

7.  Prediction of native-state hydrogen exchange from perfectly funneled energy landscapes.

Authors:  Patricio O Craig; Joachim Lätzer; Patrick Weinkam; Ryan M B Hoffman; Diego U Ferreiro; Elizabeth A Komives; Peter G Wolynes
Journal:  J Am Chem Soc       Date:  2011-10-06       Impact factor: 15.419

8.  Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.

Authors:  V A Jaravine; K Rathgeb-Szabo; A T Alexandrescu
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725

9.  Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway.

Authors:  Wenbing Hu; Zhong-Yuan Kan; Leland Mayne; S Walter Englander
Journal:  Proc Natl Acad Sci U S A       Date:  2016-03-10       Impact factor: 11.205

10.  A G-rich sequence within the c-kit oncogene promoter forms a parallel G-quadruplex having asymmetric G-tetrad dynamics.

Authors:  Shang-Te Danny Hsu; Peter Varnai; Anthony Bugaut; Anthony P Reszka; Stephen Neidle; Shankar Balasubramanian
Journal:  J Am Chem Soc       Date:  2009-09-23       Impact factor: 15.419
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