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

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Title: Response to Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”.
Authors: Riback, Joshua A. (AUTHOR), Bowman, Micayla A. (AUTHOR), Zmyslowski, Adam (AUTHOR), Knoverek, Catherine R. (AUTHOR), Jumper, John (AUTHOR), Kaye, Emily B. (AUTHOR), Freed, Karl F. (AUTHOR), Clark, Patricia L. (AUTHOR), Sosnick, Tobin R. (AUTHOR)
Source: Science (pre-March 2025). 8/31/2018, Vol. 361 Issue 6405, p1-3. 3p. 2 Graphs.
Abstract: Best et al. claim that we provide no convincing basis to assert that a discrepancy remains between FRETand 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. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Response to Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”.
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  Data: <searchLink fieldCode="AR" term="%22Riback%2C+Joshua+A%2E%22">Riback, Joshua A.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bowman%2C+Micayla+A%2E%22">Bowman, Micayla A.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zmyslowski%2C+Adam%22">Zmyslowski, Adam</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Knoverek%2C+Catherine+R%2E%22">Knoverek, Catherine R.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Jumper%2C+John%22">Jumper, John</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kaye%2C+Emily+B%2E%22">Kaye, Emily B.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Freed%2C+Karl+F%2E%22">Freed, Karl F.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Clark%2C+Patricia+L%2E%22">Clark, Patricia L.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Sosnick%2C+Tobin+R%2E%22">Sosnick, Tobin R.</searchLink> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 8/31/2018, Vol. 361 Issue 6405, p1-3. 3p. 2 Graphs.
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Best et al. claim that we provide no convincing basis to assert that a discrepancy remains between FRETand 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. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
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  Group: Ab
  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1126/science.aar7949
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      – Code: eng
        Text: English
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      – TitleFull: Response to Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”.
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            – D: 31
              M: 08
              Text: 8/31/2018
              Type: published
              Y: 2018
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