Advanced

The Dispersion of Water Proton Spin-Lattice Relaxation Rates in Aqueous Human Protein HC (alpha(1)-Microglobulin) Solutions

Dobies, Maria; Kozak, Maciej; Jurga, Stefan and Grubb, Anders LU (2009) In Protein Peptide Letters 16(12). p.1496-1503
Abstract
The H-1 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 H-1 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 H-1 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 H-1 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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
H-1, NMRD, model-free, Human protein HC (alpha(1)-microglobulin), fast field cycling
in
Protein Peptide Letters
volume
16
issue
12
pages
1496 - 1503
publisher
Bentham Science Publishers
external identifiers
  • wos:000271620200013
ISSN
0929-8665
language
English
LU publication?
yes
id
09f04eaa-e1e5-4766-ae53-97009f043dfe (old id 1518680)
date added to LUP
2009-12-28 14:50:49
date last changed
2016-04-15 20:27:19
@article{09f04eaa-e1e5-4766-ae53-97009f043dfe,
  abstract     = {The H-1 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 H-1 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.},
  author       = {Dobies, Maria and Kozak, Maciej and Jurga, Stefan and Grubb, Anders},
  issn         = {0929-8665},
  keyword      = {H-1,NMRD,model-free,Human protein HC (alpha(1)-microglobulin),fast field cycling},
  language     = {eng},
  number       = {12},
  pages        = {1496--1503},
  publisher    = {Bentham Science Publishers},
  series       = {Protein Peptide Letters},
  title        = {The Dispersion of Water Proton Spin-Lattice Relaxation Rates in Aqueous Human Protein HC (alpha(1)-Microglobulin) Solutions},
  volume       = {16},
  year         = {2009},
}