Literature DB >> 17292402

Fully reduced ribonuclease A does not expand at high denaturant concentration or temperature.

Jaby Jacob1, Robin S Dothager, P Thiyagarajan, Tobin R Sosnick.   

Abstract

The dimensions of a denatured protein, fully reduced ribonuclease A (r-RNase A), have been measured using synchrotron-based small angle X-ray scattering. The radius of gyration, 34-35 A, is unchanged from 0-6 M guanidinium chloride and from 20-90 degrees C at pH 2.5, and agrees with the known scaling behavior for a multitude of chemically denatured states. The polypeptide is behaving as a statistical coil in the non-interacting, high-temperature limit.

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Year:  2007        PMID: 17292402     DOI: 10.1016/j.jmb.2007.01.012

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  30 in total

1.  From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.

Authors:  Sonja Müller-Späth; Andrea Soranno; Verena Hirschfeld; Hagen Hofmann; Stefan Rüegger; Luc Reymond; Daniel Nettels; Benjamin Schuler
Journal:  Proc Natl Acad Sci U S A       Date:  2010-07-16       Impact factor: 11.205

2.  Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.

Authors:  Tae Yeon Yoo; Steve P Meisburger; James Hinshaw; Lois Pollack; Gilad Haran; Tobin R Sosnick; Kevin Plaxco
Journal:  J Mol Biol       Date:  2012-01-27       Impact factor: 5.469

3.  Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins.

Authors:  Yuanyuan Wang; Jill Trewhella; David P Goldenberg
Journal:  J Mol Biol       Date:  2008-02-14       Impact factor: 5.469

Review 4.  Kinetic barriers and the role of topology in protein and RNA folding.

Authors:  Tobin R Sosnick
Journal:  Protein Sci       Date:  2008-05-23       Impact factor: 6.725

5.  Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

Authors:  Daniel Nettels; Sonja Müller-Späth; Frank Küster; Hagen Hofmann; Dominik Haenni; Stefan Rüegger; Luc Reymond; Armin Hoffmann; Jan Kubelka; Benjamin Heinz; Klaus Gast; Robert B Best; Benjamin Schuler
Journal:  Proc Natl Acad Sci U S A       Date:  2009-11-20       Impact factor: 11.205

6.  Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching.

Authors:  Daniel Johansen; Cy M J Jeffries; Boualem Hammouda; Jill Trewhella; David P Goldenberg
Journal:  Biophys J       Date:  2011-02-16       Impact factor: 4.033

7.  Fractal dimension of an intrinsically disordered protein: small-angle X-ray scattering and computational study of the bacteriophage λ N protein.

Authors:  Daniel Johansen; Jill Trewhella; David P Goldenberg
Journal:  Protein Sci       Date:  2011-10-26       Impact factor: 6.725

8.  Benchmarking all-atom simulations using hydrogen exchange.

Authors:  John J Skinner; Wookyung Yu; Elizabeth K Gichana; Michael C Baxa; James R Hinshaw; Karl F Freed; Tobin R Sosnick
Journal:  Proc Natl Acad Sci U S A       Date:  2014-10-27       Impact factor: 11.205

9.  Protein folding, protein collapse, and tanford's transfer model: lessons from single-molecule FRET.

Authors:  Guy Ziv; Gilad Haran
Journal:  J Am Chem Soc       Date:  2009-03-04       Impact factor: 15.419

10.  Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations.

Authors:  Gül H Zerze; Robert B Best; Jeetain Mittal
Journal:  J Phys Chem B       Date:  2015-11-10       Impact factor: 2.991

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