Literature DB >> 30166460

Response to Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water".

Joshua A Riback1, Micayla A Bowman2, Adam Zmyslowski3, Catherine R Knoverek2, John Jumper3,4, Emily B Kaye2, Karl F Freed4, Patricia L Clark5, Tobin R Sosnick6,7.   

Abstract

Best et al claim that we provide no convincing basis to assert that a discrepancy remains between FRET and SAXS results on the dimensions of disordered proteins under physiological conditions. We maintain that a clear discrepancy is apparent in our and other recent publications, including results shown in the Best et al comment. A plausible origin is fluorophore interactions in FRET experiments.
Copyright © 2018, American Association for the Advancement of Science.

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Year:  2018        PMID: 30166460     DOI: 10.1126/science.aar7949

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  15 in total

1.  PET and FRET utility of an amino acid pair: tryptophan and 4-cyanotryptophan.

Authors:  Ismail A Ahmed; Jeffrey M Rodgers; Christina Eng; Thomas Troxler; Feng Gai
Journal:  Phys Chem Chem Phys       Date:  2019-06-10       Impact factor: 3.676

2.  The combined force field-sampling problem in simulations of disordered amyloid-β peptides.

Authors:  James Lincoff; Sukanya Sasmal; Teresa Head-Gordon
Journal:  J Chem Phys       Date:  2019-03-14       Impact factor: 3.488

3.  Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.

Authors:  Joshua A Riback; Micayla A Bowman; Adam M Zmyslowski; Kevin W Plaxco; Patricia L Clark; Tobin R Sosnick
Journal:  Proc Natl Acad Sci U S A       Date:  2019-04-16       Impact factor: 11.205

4.  Binding Affinity and Function of the Extremely Disordered Protein Complex Containing Human Linker Histone H1.0 and Its Chaperone ProTα.

Authors:  Hanqiao Feng; Bing-Rui Zhou; Yawen Bai
Journal:  Biochemistry       Date:  2018-11-19       Impact factor: 3.162

5.  Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.

Authors:  Micayla A Bowman; Joshua A Riback; Anabel Rodriguez; Hongyu Guo; Jun Li; Tobin R Sosnick; Patricia L Clark
Journal:  Proc Natl Acad Sci U S A       Date:  2020-09-02       Impact factor: 11.205

6.  Generation of the configurational ensemble of an intrinsically disordered protein from unbiased molecular dynamics simulation.

Authors:  Utsab R Shrestha; Puneet Juneja; Qiu Zhang; Viswanathan Gurumoorthy; Jose M Borreguero; Volker Urban; Xiaolin Cheng; Sai Venkatesh Pingali; Jeremy C Smith; Hugh M O'Neill; Loukas Petridis
Journal:  Proc Natl Acad Sci U S A       Date:  2019-09-23       Impact factor: 11.205

Review 7.  Emerging consensus on the collapse of unfolded and intrinsically disordered proteins in water.

Authors:  Robert B Best
Journal:  Curr Opin Struct Biol       Date:  2019-12-02       Impact factor: 6.809

8.  Origin of Internal Friction in Disordered Proteins Depends on Solvent Quality.

Authors:  Wenwei Zheng; Hagen Hofmann; Benjamin Schuler; Robert B Best
Journal:  J Phys Chem B       Date:  2018-10-02       Impact factor: 2.991

9.  Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.

Authors:  Venkatraman Ramanujam; T Reid Alderson; Iva Pritišanac; Jinfa Ying; Ad Bax
Journal:  J Magn Reson       Date:  2020-02-19       Impact factor: 2.229

Review 10.  Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.

Authors:  Patricia L Clark; Kevin W Plaxco; Tobin R Sosnick
Journal:  J Mol Biol       Date:  2020-02-07       Impact factor: 5.469

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