Biochimica et Biophysica Acta (BBA) - Protein Structure
NMR relaxation investigation of water mobility in aqueous bovine serum albumin solutions
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Fast field-cycling magnetic resonance detection of intracellular ultra-small iron oxide particles in vitro: Proof-of-concept
2020, Journal of Magnetic ResonanceCitation Excerpt :Furthermore dispersion curves may function as ‘biomarkers’ for certain pathologies and resolve differences in tissue not detected by conventional MRI. Previous work by our group and others [25,26,60,61,63–71] investigating tissue biopsies, showed potential biomarkers in a variety of pathologies that can now be investigated in vivo, using endogenous contrast FFC-MRI technology therefore has major potential to complement conventional MRI scanners in clinical diagnostics. Clinical imaging using FFC-MR has already been demonstrated in a study of acute stroke [72].
Compact NMR relaxometry of human blood and blood components
2016, TrAC - Trends in Analytical ChemistryCitation Excerpt :Another important consideration in protein relaxometry is the dependence of relaxation times on Bo field strength [30]. Early relaxation dispersion studies of serum albumin at different concentrations and temperatures suggested three rapidly-exchanging pools of water: free, translationally restricted, and rotationally bound [31]. Monitoring the temperature dependence of T1 values, thermodynamically structured water was observed to have different properties in human albumin vs. γ-globulins [32].
Proton longitudinal relaxation coupling in dynamically heterogeneous soft systems
2009, Progress in Nuclear Magnetic Resonance SpectroscopyDetermination of the effective correlation time modulating <sup>1</sup>H NMR relaxation processes of bound water in protein solutions
2008, Magnetic Resonance ImagingCitation Excerpt :The data have often been analyzed in terms of the fast chemical exchange of water molecules between free water and water bound to proteins [8–10,13,14,25–27]. In these studies, the contribution of the lifetime (τm) of water on a protein molecule to the effective correlation time modulating the relaxation process was neglected since it was evaluated to be larger than the rotational correlation time (τr) of protein molecules [8–10,17,21,22,26]. The Cole–Cole expression was used for the estimation of the τr modulating the relaxation mechanism of bound water [8,28,29].
1. Features of the state of bound water in Bio-Objects as an example of the nature of sorbed in swelling sorbents
2007, Interface Science and TechnologyProton T<inf>1</inf> and T<inf>2</inf> relaxivities of serum proteins
2004, Magnetic Resonance Imaging