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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03418naa a2200373 4500 | |
| 001 | oai:lup.lub.lu.se:f9fae998-91b1-42af-9070-13472fad9b50 | |
| 003 | SwePub | |
| 008 | 181022s2019 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://lup.lub.lu.se/record/f9fae998-91b1-42af-9070-13472fad9b502 URI |
| 024 | 7 | a https://doi.org/10.1002/cphc.2018006262 DOI |
| 040 | a (SwePub)lu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Wallerstein, Johanu Lund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)bpc-jwl |
| 245 | 1 0 | a Minute Additions of DMSO Affect Protein Dynamics Measurements by NMR Relaxation Experiments through Significant Changes in Solvent Viscosity |
| 264 | c 2018-09-03 | |
| 264 | 1 | b Wiley,c 2019 |
| 520 | a Studies of protein−ligand binding often rely on dissolving the ligand in dimethyl sulfoxide (DMSO) to achieve sufficient solubility, and then titrating the ligand solution into the protein solution. As a result, the final protein−ligand solution contains small amounts of DMSO in the buffer. Here we report how the addition of DMSO impacts studies of protein conformational dynamics. We used 15N NMR relaxation to compare the rotational diffusion correlation time (τC) of proteins in aqueous buffer with and without DMSO. We found that τC scales with the viscosity of the water−DMSO mixture, which depends sensitively on the amount of DMSO and varies by a factor of 2 across the relevant concentration range. NMR relaxation studies of side chains dynamics are commonly interpreted using τC as a fixed parameter, obtained from backbone 15N relaxation data acquired on a separate sample. Model-free calculations show that errors in τC, arising from mismatched DMSO concentration between samples, lead to significant errors in order parameters. Our results highlight the importance of determining τC for each sample or carefully matching the DMSO concentrations between samples. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
| 653 | a drug design | |
| 653 | a ligand binding | |
| 653 | a order parameter | |
| 653 | a rotational diffusion | |
| 653 | a side-chain dynamics | |
| 700 | 1 | a Akke, Mikaelu Lund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)fkm2-mak |
| 710 | 2 | a Biofysikalisk kemib Centrum för Molekylär Proteinvetenskap4 org |
| 773 | 0 | t ChemPhysChemd : Wileyg 20:2, s. 326-332q 20:2<326-332x 1439-4235 |
| 856 | 4 | u http://dx.doi.org/10.1002/cphc.201800626y FULLTEXT |
| 856 | 4 | u https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cphc.201800626 |
| 856 | 4 8 | u https://lup.lub.lu.se/record/f9fae998-91b1-42af-9070-13472fad9b50 |
| 856 | 4 8 | u https://doi.org/10.1002/cphc.201800626 |
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