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

Publication type:
Journal article
Metadata:
Autoren
  • Gustavo Fuertes
  • Niccolo Banterle
  • Kiersten M Ruff
  • Aritra Chowdhury
  • Rohit V Pappu
  • Dmitri I Svergun
  • Edward A Lemke
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000443547000004&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1126/science.aau8230
eISSN
1095-9203
Externe Identifier
  • Clarivate Analytics Document Solution ID: GS3UB
  • PubMed Identifier: 30166461
ISSN
0036-8075
Ausgabe der Veröffentlichung
6405
Zeitschrift
SCIENCE
Artikelnummer
ARTN aau8230
Datum der Veröffentlichung
2018
Status
Published
Titel
Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"
Sub types
  • Editorial Material
Ausgabe der Zeitschrift
361

Data source: Web of Science (Lite)

Other metadata sources:
Abstract
<jats:p> Editors at <jats:italic>Science</jats:italic> requested our input on the above discussion (comment by Best <jats:italic>et al</jats:italic> . and response by Riback <jats:italic>et al</jats:italic> .) because both sets of authors use our data from Fuertes <jats:italic>et al</jats:italic> . (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fluctuations that is intrinsic to finite-sized, heteropolymeric IDPs. Accounting for this decoupling resolves the discrepant inferences between the two methods, thus making a case for the utility of both methods. </jats:p>
Autoren
  • Gustavo Fuertes
  • Niccolo Banterle
  • Kiersten M Ruff
  • Aritra Chowdhury
  • Rohit V Pappu
  • Dmitri I Svergun
  • Edward A Lemke
DOI
10.1126/science.aau8230
eISSN
1095-9203
ISSN
0036-8075
Ausgabe der Veröffentlichung
6405
Zeitschrift
Science
Sprache
en
Datum der Veröffentlichung
2018
Status
Published
Herausgeber
American Association for the Advancement of Science (AAAS)
Herausgeber URL
http://dx.doi.org/10.1126/science.aau8230
Datum der Datenerfassung
2024
Titel
Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”
Ausgabe der Zeitschrift
361

Data source: Crossref

Abstract
Editors at <i>Science</i> requested our input on the above discussion (comment by Best <i>et al</i> and response by Riback <i>et al</i>) because both sets of authors use our data from Fuertes <i>et al</i> (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fluctuations that is intrinsic to finite-sized, heteropolymeric IDPs. Accounting for this decoupling resolves the discrepant inferences between the two methods, thus making a case for the utility of both methods.
Addresses
  • European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Autoren
  • Gustavo Fuertes
  • Niccolo Banterle
  • Kiersten M Ruff
  • Aritra Chowdhury
  • Rohit V Pappu
  • Dmitri I Svergun
  • Edward A Lemke
DOI
10.1126/science.aau8230
eISSN
1095-9203
Externe Identifier
  • PubMed Identifier: 30166461
  • PubMed Central ID: PMC7611747
Funding acknowledgements
  • NINDS NIH HHS: R01 NS056114
  • European Research Council: 646451
  • European Research Council: 653706
Open access
false
ISSN
0036-8075
Ausgabe der Veröffentlichung
6405
Zeitschrift
Science (New York, N.Y.)
Schlüsselwörter
  • Water
  • X-Ray Diffraction
  • Protein Conformation
  • Scattering, Small Angle
  • Hydrophobic and Hydrophilic Interactions
  • Intrinsically Disordered Proteins
Sprache
eng
Medium
Print
Paginierung
eaau8230
Datum der Veröffentlichung
2018
Status
Published
Datum der Datenerfassung
2018
Titel
Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water".
Sub types
  • article-commentary
  • Comment
  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
361

Files

https://science.sciencemag.org/content/sci/361/6405/eaau8230.full.pdf https://europepmc.org/articles/PMC7611747?pdf=render

Data source: Europe PubMed Central

Abstract
Editors at Science requested our input on the above discussion (comment by Best et al and response by Riback et al) because both sets of authors use our data from Fuertes et al (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fluctuations that is intrinsic to finite-sized, heteropolymeric IDPs. Accounting for this decoupling resolves the discrepant inferences between the two methods, thus making a case for the utility of both methods.
Date of acceptance
2018
Autoren
  • Gustavo Fuertes
  • Niccolo Banterle
  • Kiersten M Ruff
  • Aritra Chowdhury
  • Rohit V Pappu
  • Dmitri I Svergun
  • Edward A Lemke
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/30166461
DOI
10.1126/science.aau8230
eISSN
1095-9203
Externe Identifier
  • NIH Manuscript Submission ID: EMS134952
  • PubMed Central ID: PMC7611747
Funding acknowledgements
  • European Research Council: 646451
  • NINDS NIH HHS: R01 NS056114
Ausgabe der Veröffentlichung
6405
Zeitschrift
Science
Schlüsselwörter
  • Hydrophobic and Hydrophilic Interactions
  • Intrinsically Disordered Proteins
  • Protein Conformation
  • Scattering, Small Angle
  • Water
  • X-Ray Diffraction
Sprache
eng
Country
United States
PII
361/6405/eaau8230
Datum der Veröffentlichung
2018
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2018
Titel
Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water".
Sub types
  • Journal Article
  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't
  • Comment
Ausgabe der Zeitschrift
361

Data source: PubMed

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