6533b853fe1ef96bd12ac3f5
RESEARCH PRODUCT
Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”
Kiersten M. RuffAritra ChowdhuryDmitri I. SvergunEdward A. LemkeNiccolò BanterleRohit V. PappuGustavo Fuertessubject
0301 basic medicinePhysicsMultidisciplinarySmall-angle X-ray scatteringScattering010402 general chemistryIntrinsically disordered proteins01 natural sciences0104 chemical sciences03 medical and health sciences030104 developmental biologyFörster resonance energy transferStatistical physicsDecoupling (electronics)description
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2018-08-31 | Science |