Immobilized protein solute, approximately 20 wt %, alters the longitudinal and transverse nuclear magnetic relaxation rates 1/T1 and 1/T2 of solvent water protons in a manner that makes their values indistinguishable from those of a typical human tissue. There is now a quantitative theory at the molecular level (S.H. Koenig and R. D. Brown III (1993) Magn. Reson. Med. 30:685–695) that accounts for this, as a function of magnetic field strength, in terms of several distinguishable classes of water-binding sites at the protein-water interface at which significant relaxation and solute-solvent transfer of proton Zeeman energy occur. We review the arguments that these several classes of sites, characterized by widely disparate values of the res...
Water is fundamental to all aspects of protein function including folding, stability, catalysis, and...
The deuterated hydration shells of bovine serum (BSA) albumin, and purple membrane sheets have been ...
Water-protein interactions help to maintain flexible conformation conditions which are required for ...
Immobilized protein solute, approximately 20 wt %, alters the longitudinal and transverse nuclear ma...
Nuclear magnetic resonance (NMR) measurements provide both structural and dynamical information abou...
The inflection frequency of the deuteron magnetic relaxation dispersion from water in rotationally i...
AbstractRotational immobilization of proteins permits characterization of the internal peptide and w...
AbstractThe water-proton spin-lattice relaxation rate constant, 1/T1, was measured as a function of ...
Kimmich and co-workers (cf., Winter, F., and R. Kimmich. 1982. Biochim. Biophys. Acta. 719:292–298) ...
As demonstrated by bulk water proton T$\sb{1\rho}$ dispersion results, protein crosslinking revealed...
The results presented in this thesis demonstrate that the magnetic relaxation dispersion (MRD) techn...
Proteins in solution affect the structural and dynamic properties of the bulk water at the protein-w...
An extensive set of water-H magnetic relaxation dispersion (MRD) data are presented for aqueous agar...
Water is fundamental to all aspects of protein function including folding, stability, catalysis, and...
Water-protein interactions help to maintain flexible conformation conditions which are required for ...
Water is fundamental to all aspects of protein function including folding, stability, catalysis, and...
The deuterated hydration shells of bovine serum (BSA) albumin, and purple membrane sheets have been ...
Water-protein interactions help to maintain flexible conformation conditions which are required for ...
Immobilized protein solute, approximately 20 wt %, alters the longitudinal and transverse nuclear ma...
Nuclear magnetic resonance (NMR) measurements provide both structural and dynamical information abou...
The inflection frequency of the deuteron magnetic relaxation dispersion from water in rotationally i...
AbstractRotational immobilization of proteins permits characterization of the internal peptide and w...
AbstractThe water-proton spin-lattice relaxation rate constant, 1/T1, was measured as a function of ...
Kimmich and co-workers (cf., Winter, F., and R. Kimmich. 1982. Biochim. Biophys. Acta. 719:292–298) ...
As demonstrated by bulk water proton T$\sb{1\rho}$ dispersion results, protein crosslinking revealed...
The results presented in this thesis demonstrate that the magnetic relaxation dispersion (MRD) techn...
Proteins in solution affect the structural and dynamic properties of the bulk water at the protein-w...
An extensive set of water-H magnetic relaxation dispersion (MRD) data are presented for aqueous agar...
Water is fundamental to all aspects of protein function including folding, stability, catalysis, and...
Water-protein interactions help to maintain flexible conformation conditions which are required for ...
Water is fundamental to all aspects of protein function including folding, stability, catalysis, and...
The deuterated hydration shells of bovine serum (BSA) albumin, and purple membrane sheets have been ...
Water-protein interactions help to maintain flexible conformation conditions which are required for ...