Molecular dynamics of proteins investigated by NMR relaxation methods

2014
journal article
article
3
dc.abstract.enThe nuclear magnetic resonance relaxation times of solvent water nuclei are known to decrease upon addition of diamagnetic solute protein. For this reason NMR relaxation methods are able to provide information on molecular dynamics changes of water protons and their interaction with macromolecules' surfaces. We present results of measurements of relaxation rates R1 = 1/T1, R2 = 1/T2 and R1ρ = 1/T1ρ in the rotating frame for three proteins: chicken egg white lysozyme, egg white albumin, and bovine serum albumin, obtained at proton resonant frequency of 60 MHz. Besides the relaxation rates dependences on concentration in the 4-23% (g/100 g solution) range, the analysis of the Carr-Purcell-Meiboom-Gill CPMG multi-echo T2 experiments with variable pulse rate τ was performed. The dependences of relaxation rates on protein concentration are linear at low concentration. When protein concentration increases the slope of the straight line rapidly changes at so-called "critical" concentration which depends on MW of the diluted protein. Investigated dispersion of T2, obtained using the CPMG method with a variable pulse rate, for concentrations higher and lower than the "critical" one, exhibits unequal behavior. At high concentration one-exponential curves and at low concentration two-exponential curves correspond closely with experimental data. The obtained parameters of exponents allow an estimation of the ratio of the amount of water with the determined motion freedom, that is free and bounded water, in solution. We showed that the CPMG dispersion method applied to aqueous protein solutions may widen the current understanding of the nature of molecular dynamics of hydrated water protons in non-perturbed environment.pl
dc.affiliationWydział Fizyki, Astronomii i Informatyki Stosowanej : Instytut Fizyki im. Mariana Smoluchowskiegopl
dc.contributor.authorWierzuchowska, D.pl
dc.contributor.authorBlicharska, Barbara - 127355 pl
dc.date.accessioned2015-12-08T18:31:08Z
dc.date.available2015-12-08T18:31:08Z
dc.date.issued2014pl
dc.date.openaccess0
dc.description.accesstimew momencie opublikowania
dc.description.admin[AB] Blicharska, Barbara [SAP11003908] 50000139
dc.description.number4pl
dc.description.physical907-910pl
dc.description.publication0,2pl
dc.description.versionostateczna wersja wydawcy
dc.description.volume125pl
dc.identifier.doi10.12693/APhysPolA.125.907pl
dc.identifier.eissn1898-794Xpl
dc.identifier.issn0587-4246pl
dc.identifier.projectROD UJ / Ppl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/17853
dc.languageengpl
dc.language.containerengpl
dc.rightsUdzielam licencji. Uznanie autorstwa - Użycie niekomercyjne - Bez utworów zależnych 4.0 Międzynarodowa*
dc.rights.licenceOTHER
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.pl*
dc.share.typeotwarte czasopismo
dc.subtypeArticlepl
dc.titleMolecular dynamics of proteins investigated by NMR relaxation methodspl
dc.title.journalActa Physica Polonica. Apl
dc.title.volumeProceedings of the XLVIIIth Zakopane School of Physics International Symposium Breaking Frontiers: Submicron Structures in Physics and Biology, Zakopane, Poland, May 20-25, 2013 and Proceedings of the 15th International Conference on Defects Recognition, Imaging and Physics in Semiconductors Warsaw, Poland, September 15-19, 2013pl
dc.typeJournalArticlepl
dspace.entity.typePublication
dc.abstract.enpl
The nuclear magnetic resonance relaxation times of solvent water nuclei are known to decrease upon addition of diamagnetic solute protein. For this reason NMR relaxation methods are able to provide information on molecular dynamics changes of water protons and their interaction with macromolecules' surfaces. We present results of measurements of relaxation rates R1 = 1/T1, R2 = 1/T2 and R1ρ = 1/T1ρ in the rotating frame for three proteins: chicken egg white lysozyme, egg white albumin, and bovine serum albumin, obtained at proton resonant frequency of 60 MHz. Besides the relaxation rates dependences on concentration in the 4-23% (g/100 g solution) range, the analysis of the Carr-Purcell-Meiboom-Gill CPMG multi-echo T2 experiments with variable pulse rate τ was performed. The dependences of relaxation rates on protein concentration are linear at low concentration. When protein concentration increases the slope of the straight line rapidly changes at so-called "critical" concentration which depends on MW of the diluted protein. Investigated dispersion of T2, obtained using the CPMG method with a variable pulse rate, for concentrations higher and lower than the "critical" one, exhibits unequal behavior. At high concentration one-exponential curves and at low concentration two-exponential curves correspond closely with experimental data. The obtained parameters of exponents allow an estimation of the ratio of the amount of water with the determined motion freedom, that is free and bounded water, in solution. We showed that the CPMG dispersion method applied to aqueous protein solutions may widen the current understanding of the nature of molecular dynamics of hydrated water protons in non-perturbed environment.
dc.affiliationpl
Wydział Fizyki, Astronomii i Informatyki Stosowanej : Instytut Fizyki im. Mariana Smoluchowskiego
dc.contributor.authorpl
Wierzuchowska, D.
dc.contributor.authorpl
Blicharska, Barbara - 127355
dc.date.accessioned
2015-12-08T18:31:08Z
dc.date.available
2015-12-08T18:31:08Z
dc.date.issuedpl
2014
dc.date.openaccess
0
dc.description.accesstime
w momencie opublikowania
dc.description.admin
[AB] Blicharska, Barbara [SAP11003908] 50000139
dc.description.numberpl
4
dc.description.physicalpl
907-910
dc.description.publicationpl
0,2
dc.description.version
ostateczna wersja wydawcy
dc.description.volumepl
125
dc.identifier.doipl
10.12693/APhysPolA.125.907
dc.identifier.eissnpl
1898-794X
dc.identifier.issnpl
0587-4246
dc.identifier.projectpl
ROD UJ / P
dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/17853
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Udzielam licencji. Uznanie autorstwa - Użycie niekomercyjne - Bez utworów zależnych 4.0 Międzynarodowa
dc.rights.licence
OTHER
dc.rights.uri*
http://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.pl
dc.share.type
otwarte czasopismo
dc.subtypepl
Article
dc.titlepl
Molecular dynamics of proteins investigated by NMR relaxation methods
dc.title.journalpl
Acta Physica Polonica. A
dc.title.volumepl
Proceedings of the XLVIIIth Zakopane School of Physics International Symposium Breaking Frontiers: Submicron Structures in Physics and Biology, Zakopane, Poland, May 20-25, 2013 and Proceedings of the 15th International Conference on Defects Recognition, Imaging and Physics in Semiconductors Warsaw, Poland, September 15-19, 2013
dc.typepl
JournalArticle
dspace.entity.type
Publication
Affiliations

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