Literature DB >> 17602628

Quantitative analysis of nonequilibrium, denaturant-dependent protein folding transitions.

Denis Erilov1, Chasper Puorger, Rudi Glockshuber.   

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Year:  2007        PMID: 17602628     DOI: 10.1021/ja0718927

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


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  3 in total

1.  Donor strand sequence, rather than donor strand orientation, determines the stability and non-equilibrium folding of the type 1 pilus subunit FimA.

Authors:  Dawid Zyla; Blanca Echeverria; Rudi Glockshuber
Journal:  J Biol Chem       Date:  2020-07-10       Impact factor: 5.157

2.  Engineering a Hyperstable Yersinia pestis Outer Membrane Protein Ail Using Thermodynamic Design.

Authors:  Anjana George; Roshika Ravi; Pankaj Bharat Tiwari; Shashank Ranjan Srivastava; Vikas Jain; Radhakrishnan Mahalakshmi
Journal:  J Am Chem Soc       Date:  2022-01-21       Impact factor: 15.419

3.  Alternative folding to a monomer or homopolymer is a common feature of the type 1 pilus subunit FimA from enteroinvasive bacteria.

Authors:  Dawid S Żyła; Andrea E Prota; Guido Capitani; Rudi Glockshuber
Journal:  J Biol Chem       Date:  2019-05-24       Impact factor: 5.157

  3 in total

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