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The dispersion of water proton spin-lattice relaxation rates in aqueous human protein HC (alpha1-microglobulin) solutions

Dobies, Maria; Kozak, Maciej; Jurga, Stefan and Grubb, Anders LU (2009) In Protein and Peptide Letters 16(12). p.1496-1503
Abstract

The (1)H NMR Fast Field Cycling relaxometry was applied to study the molecular dynamics of the human protein HC (alpha (1)-microglobulin), its hydration and aggregation in solution state. The (1)H NMRD data have revealed the complex nature of the water/protein HC system resulting from the co-existence of monomer and dimer forms of the protein in solution as well as the presence of oligosaccharides linked to the polypeptide chain. A comparison of the average correlation time values <tau (c)> obtained from the model-free fits with the values predicted on the basis of hydrodynamic tau (r) theory, suggests that the dynamics in solution state is governed mainly by the dimer form of the protein HC (the dominant contribution to the water... (More)

The (1)H NMR Fast Field Cycling relaxometry was applied to study the molecular dynamics of the human protein HC (alpha (1)-microglobulin), its hydration and aggregation in solution state. The (1)H NMRD data have revealed the complex nature of the water/protein HC system resulting from the co-existence of monomer and dimer forms of the protein in solution as well as the presence of oligosaccharides linked to the polypeptide chain. A comparison of the average correlation time values <tau (c)> obtained from the model-free fits with the values predicted on the basis of hydrodynamic tau (r) theory, suggests that the dynamics in solution state is governed mainly by the dimer form of the protein HC (the dominant contribution to the water proton-spin lattice relaxation comes from exchanging protons from the surface of the dimer). The existence of small number of oligomeric forms of the protein HC in solutions is postulated because of the two-step shape of water proton spin-lattice relaxation rate dispersion profiles.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Alpha-Globulins, Animals, Cattle, Humans, Molecular Dynamics Simulation, Protons, Solutions, Water, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
in
Protein and Peptide Letters
volume
16
issue
12
pages
8 pages
publisher
Bentham Science Publishers
external identifiers
  • scopus:73449124123
ISSN
0929-8665
DOI
10.2174/092986609789839241
language
English
LU publication?
no
id
4c590676-770b-4d7f-9f33-9d3816aa42cc
date added to LUP
2016-11-22 19:03:03
date last changed
2017-07-02 04:56:20
@article{4c590676-770b-4d7f-9f33-9d3816aa42cc,
  abstract     = {<p>The (1)H NMR Fast Field Cycling relaxometry was applied to study the molecular dynamics of the human protein HC (alpha (1)-microglobulin), its hydration and aggregation in solution state. The (1)H NMRD data have revealed the complex nature of the water/protein HC system resulting from the co-existence of monomer and dimer forms of the protein in solution as well as the presence of oligosaccharides linked to the polypeptide chain. A comparison of the average correlation time values &lt;tau (c)&gt; obtained from the model-free fits with the values predicted on the basis of hydrodynamic tau (r) theory, suggests that the dynamics in solution state is governed mainly by the dimer form of the protein HC (the dominant contribution to the water proton-spin lattice relaxation comes from exchanging protons from the surface of the dimer). The existence of small number of oligomeric forms of the protein HC in solutions is postulated because of the two-step shape of water proton spin-lattice relaxation rate dispersion profiles.</p>},
  author       = {Dobies, Maria and Kozak, Maciej and Jurga, Stefan and Grubb, Anders},
  issn         = {0929-8665},
  keyword      = {Alpha-Globulins,Animals,Cattle,Humans,Molecular Dynamics Simulation,Protons,Solutions,Water,Comparative Study,Journal Article,Research Support, Non-U.S. Gov't},
  language     = {eng},
  number       = {12},
  pages        = {1496--1503},
  publisher    = {Bentham Science Publishers},
  series       = {Protein and Peptide Letters},
  title        = {The dispersion of water proton spin-lattice relaxation rates in aqueous human protein HC (alpha1-microglobulin) solutions},
  url          = {http://dx.doi.org/10.2174/092986609789839241},
  volume       = {16},
  year         = {2009},
}