Literature DB >> 9261079

Touring the landscapes: partially folded proteins examined by hydrogen exchange.

A K Chamberlain1, S Marqusee.   

Abstract

Recent studies on Escherichia coli ribonuclease H and several other proteins reveal a specific region in each protein that remains structured in partially folded conformations. These regions play a dominant role in determining the fold and stability of the protein.

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Year:  1997        PMID： 9261079     DOI： 10.1016/s0969-2126(97)00240-2

Source DB:  PubMed          Journal:  Structure        ISSN： 0969-2126            Impact factor:   5.006


  19 in total

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2.  An amino acid code for protein folding.

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6.  A two-stage differential hydrogen deuterium exchange method for the rapid characterization of protein/ligand interactions.

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8.  Tertiary interactions determine the accuracy of RNA folding.

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10.  The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.

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Journal:  Protein Sci       Date:  1999-08       Impact factor: 6.725
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