guest ::
| Home > Publications database > FRET Dyes Significantly Affect SAXS Intensities of Proteins > print |
| 001 | 888467 | ||
| 005 | 20210130010943.0 | ||
| 024 | 7 | _ | |a 10.1002/ijch.202000007 |2 doi |
| 024 | 7 | _ | |a 0021-2148 |2 ISSN |
| 024 | 7 | _ | |a 1869-5868 |2 ISSN |
| 024 | 7 | _ | |a 2128/26554 |2 Handle |
| 024 | 7 | _ | |a WOS:000550773000008 |2 WOS |
| 037 | _ | _ | |a FZJ-2020-04935 |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Reinartz, Ines |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a FRET Dyes Significantly Affect SAXS Intensities of Proteins |
| 260 | _ | _ | |a Weinheim |c 2020 |b Wiley-VCH |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1608045321_18852 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Structural analyses in biophysics aim at revealing a relationship between a molecule's dynamic structure and its physiological function. Förster resonance energy transfer (FRET) and small‐angle X‐ray scattering (SAXS) are complementary experimental approaches to this. Their concomitant application in combined studies has recently opened a lively debate on how to interpret FRET measurements in the light of SAXS data with the popular example of the radius of gyration, commonly derived from both FRET and SAXS. There still is a lack of understanding in how to mutually relate and interpret quantities equally obtained from FRET or SAXS, and to what extent FRET dyes affect SAXS intensities in combined applications. In the present work, we examine the interplay of FRET and SAXS from a computational simulation perspective. Molecular simulations are a valuable complement to experimental approaches and supply instructive information on dynamics. As FRET depends not only on the mutual separation but also on the relative orientations, the dynamics, and therefore also the shapes of the dyes, we utilize a novel method for simulating FRET‐dye‐labeled proteins to investigate these aspects in atomic detail. We perform structure‐based simulations of four different proteins with and without dyes in both folded and unfolded conformations. In‐silico derived radii of gyration are different with and without dyes and depend on the chosen dye pair. The dyes apparently influence the dynamics of unfolded systems. We find that FRET dyes attached to a protein have a significant impact on theoretical SAXS intensities calculated from simulated structures, especially for small proteins. Radii of gyration from FRET and SAXS deviate systematically, which points to further underlying mechanisms beyond prevalent explanation approaches. |
| 536 | _ | _ | |a 511 - Computational Science and Mathematical Methods (POF3-511) |0 G:(DE-HGF)POF3-511 |c POF3-511 |f POF III |x 0 |
| 536 | _ | _ | |a Forschergruppe Schug (hkf6_20200501) |0 G:(DE-Juel1)hkf6_20200501 |c hkf6_20200501 |f Forschergruppe Schug |x 1 |
| 588 | _ | _ | |a Dataset connected to CrossRef |
| 700 | 1 | _ | |a Weiel, Marie |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Schug, Alexander |0 P:(DE-Juel1)173652 |b 2 |e Corresponding author |
| 773 | _ | _ | |a 10.1002/ijch.202000007 |g Vol. 60, no. 7, p. 725 - 734 |0 PERI:(DE-600)2066481-3 |n 7 |p 725 - 734 |t Israel journal of chemistry |v 60 |y 2020 |x 1869-5868 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/888467/files/ijch.202000007.pdf |y OpenAccess |
| 909 | C | O | |o oai:juser.fz-juelich.de:888467 |p openaire |p open_access |p VDB |p driver |p dnbdelivery |
| 910 | 1 | _ | |a Forschungszentrum Jülich |0 I:(DE-588b)5008462-8 |k FZJ |b 2 |6 P:(DE-Juel1)173652 |
| 913 | 1 | _ | |a DE-HGF |b Key Technologies |1 G:(DE-HGF)POF3-510 |0 G:(DE-HGF)POF3-511 |2 G:(DE-HGF)POF3-500 |v Computational Science and Mathematical Methods |x 0 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF3 |l Supercomputing & Big Data |
| 914 | 1 | _ | |y 2020 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |d 2020-09-04 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |d 2020-09-04 |
| 915 | _ | _ | |a Creative Commons Attribution CC BY 4.0 |0 LIC:(DE-HGF)CCBY4 |2 HGFVOC |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0600 |2 StatID |b Ebsco Academic Search |d 2020-09-04 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1150 |2 StatID |b Current Contents - Physical, Chemical and Earth Sciences |d 2020-09-04 |
| 915 | _ | _ | |a DEAL Wiley |0 StatID:(DE-HGF)3001 |2 StatID |d 2020-09-04 |w ger |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0113 |2 StatID |b Science Citation Index Expanded |d 2020-09-04 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |d 2020-09-04 |
| 915 | _ | _ | |a IF < 5 |0 StatID:(DE-HGF)9900 |2 StatID |d 2020-09-04 |
| 915 | _ | _ | |a OpenAccess |0 StatID:(DE-HGF)0510 |2 StatID |
| 915 | _ | _ | |a Peer Review |0 StatID:(DE-HGF)0030 |2 StatID |b ASC |d 2020-09-04 |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |b ISR J CHEM : 2018 |d 2020-09-04 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0160 |2 StatID |b Essential Science Indicators |d 2020-09-04 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Clarivate Analytics Master Journal List |d 2020-09-04 |
| 920 | 1 | _ | |0 I:(DE-Juel1)JSC-20090406 |k JSC |l Jülich Supercomputing Center |x 0 |
| 920 | 1 | _ | |0 I:(DE-Juel1)NIC-20090406 |k NIC |l John von Neumann - Institut für Computing |x 1 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)JSC-20090406 |
| 980 | _ | _ | |a I:(DE-Juel1)NIC-20090406 |
| 980 | 1 | _ | |a FullTexts |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|