Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, Research Support, N.I.H., Intramural, práce podpořená grantem, komentáře
Grantová podpora
646451
European Research Council - International
R01 NS056114
NINDS NIH HHS - United States
PubMed
30166461
PubMed Central
PMC7611747
DOI
10.1126/science.aau8230
PII: 361/6405/eaau8230
Knihovny.cz E-zdroje
- MeSH
- difrakce rentgenového záření * MeSH
- hydrofobní a hydrofilní interakce MeSH
- konformace proteinů MeSH
- maloúhlový rozptyl * MeSH
- vnitřně neuspořádané proteiny MeSH
- voda MeSH
- Publikační typ
- časopisecké články MeSH
- komentáře MeSH
- práce podpořená grantem MeSH
- Research Support, N.I.H., Intramural MeSH
- Názvy látek
- vnitřně neuspořádané proteiny MeSH
- voda MeSH
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.
European Molecular Biology Laboratory 22607 Hamburg Germany
European Molecular Biology Laboratory 69117 Heidelberg Germany
Zobrazit více v PubMed
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Riback JA, et al. Science. 2017;358:238–241. PubMed PMC
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Riback JA, et al. Science. 2018;361:eaar7949. PubMed
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