Search Results - "Viles, J H"

Local Structural Plasticity of the Prion Protein. Analysis of NMR Relaxation Dynamics by Viles, John H, Donne, David, Kroon, Gerard, Prusiner, Stanley B, Cohen, Fred E, Dyson, H. Jane, Wright, Peter E

“…A template-assisted conformational change of the cellular prion protein (PrPC) from a predominantly helical structure to an amyloid-type structure with a…”
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Copper Binding to the Amyloid- beta (A beta ) Peptide Associated with Alzheimer's Disease: folding, coordination geometry, ph dependence, stoichiometry, and affinity of A beta -(1-28): insights from a range of complementary spectroscopic techniques by Syme, C D, Nadal, R C, Rigby, SEJ, Viles, J H

“…There is now direct evidence that copper is bound to amyloid- beta peptide (A beta ) in senile plaque of Alzheimer's disease. Copper is also linked with the…”
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Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism by Garnett, Anthony P, Viles, John H

“…The prion protein (PrP) is a Cu(2+) binding cell surface glycoprotein. There is increasing evidence that PrP functions as a copper transporter. In addition,…”
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Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods by Viles, J H, Duggan, B M, Zaborowski, E, Schwarzinger, S, Huntley, J J, Kroon, G J, Dyson, H J, Wright, P E

“…We present an evaluation of the accuracy and precision of relaxation rates calculated using a variety of methods, applied to data sets obtained for several…”
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Involvement of a lysine residue in the N-terminal Ni2+ and Cu2+ binding site of serum albumins : comparison with Co2+, Cd2+ and Al3 by SADLER, P. J, TUCKER, A, VILES, J. H

“…We report one-dimensional and two-dimensional 1H-NMR studies of the binding of Ni2+, Cu2+, Co2+, Cd2+ and Al3+ to defatted bovine and human serum albumins. The…”
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Copper Binding to the Prion Protein: Structural Implications of Four Identical Cooperative Binding Sites by Viles, John H., Cohen, Fred E., Prusiner, Stanely B., Goodin, David B., Wright, Peter E., Dyson, H. Jane

“…Evidence is growing to support a functional role for the prion protein (PrP) in copper metabolism. Copper ions appear to bind to the protein in a highly…”
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Structure of the Recombinant Full-Length Hamster Prion Protein PrP(29-231): The N Terminus is Highly Flexible by Donne, David G., Viles, John H., Groth, Darlene, Mehlhorn, Ingrid, James, Thomas L., Cohen, Fred E., Prusiner, Stanley B., Wright, Peter E., Dyson, H. Jane

“…The prion diseases seem to be caused by a conformational change of the prion protein (PrP) from the benign cellular from PrPCto the infectious scrapie form…”
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Observation of albumin resonances in proton nuclear magnetic resonance spectra of human blood plasma: N-terminal assignments aided by use of modified recombinant albumin by Harris, R, Patel, S U, Sadler, P J, Viles, J H

“…Two-dimensional total shift correlation spectroscopy (TOCSY) and double-quantum-filtered phase-sensitive homonuclear shift-correlated spectroscopy (DQF-COSY)…”
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Design, synthesis and structure of a zinc finger with an artificial β-turn by Viles, John H., Patel, Sunil U., Mitchell, John B.O., Moody, Claire M., Justice, David E., Uppenbrink, Julia, Doyle, Paul M., Harris, C.John, Sadler, Peter J., Thornton, Janet M.

“…We have incorporated a bicyclic β-turn mimetic (BTD; β-turn dipeptide) into a zinc finger, creating a zinc finger with an artificial β-turn. The designed…”
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Empirical rules for rationalising visible circular dichroism of Cu super(2) super(+) and Ni super(2) super(+) histidine complexes: Applications to the prion protein by Klewpatinond, M, Viles, J H

“…A natively unfolded region of the prion protein, PrP(90-126) binds Cu super(2) super(+) ions and is vital for prion propagation. Pentapeptides, acyl-GGGTH…”
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Direct detection of albumin in human blood plasma by 1H NMR spectroscopy. Complexation of nickel2 by PATEL, S. U, SADLER, P. J, TUCKER, A, VILES, J. H

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Towards meeting the paracelsus challenge: The design, synthesis, and characterization of paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein by Jones, David T., Moody, Claire M., Uppenbrink, Julia, Viles, John H., Doyle, Paul M., Harris, C. John, Pearl, Laurence H., Sadler, Peter J., Thornton, Janet M.

“…In response to the Paracelsus Challenge (Rose and Creamer, Proteins, 19:1–3, 1994), we present here the design, synthesis, and characterization of a helical…”
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Solution super(1)H NMR investigation of Zn super(2+) and Cd super(2+) binding to amyloid-beta peptide (A beta ) of Alzheimer's disease by Syme, C D, Viles, J H

“…Elevated levels of zinc super(2+) and copper super(2+) are found chelated to the amyloid-beta-peptide (A beta ) in isolated senile plaque cores of Alzheimer's…”
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NMR characterization of the pH 4 beta-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility by O'Sullivan, Denis B D, Jones, Christopher E, Abdelraheim, Salama R, Thompsett, Andrew R, Brazier, Marcus W, Toms, Harold, Brown, David R, Viles, John H

“…Prion diseases are associated with the misfolding of the PrP (prion protein) from a largely alpha-helical isoform to a beta-sheet-rich oligomer. CD has shown…”
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Multiple solution conformations of the integrin-binding cyclic pentapeptide cyclo(-Ser-D-Leu-Asp-Val-Pro-). Analysis of the (phi, psi) space available to cyclic pentapeptides by Viles, J H, Mitchell, J B, Gough, S L, Doyle, P M, Harris, C J, Sadler, P J, Thornton, J M

“…The aqueous solution structure of the cyclic pentapeptide cyclo(-Ser-D-Leu-Asp-Val-Pro-) has been determined by two-dimensional 1H-NMR spectroscopy, combined…”
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Solution structure of a biologically active cyclic LDV peptide analogue containing a type II' beta-turn mimetic by Doyle, P M, Harris, J C, Moody, C M, Sadler, P J, Sims, M, Thornton, J M, Uppenbrink, J, Viles, J H

“…The solution structure of cyclo-[Gly-Leu-Asp-Val-BTD] (BTD = beta-turn dipeptide) has been determined by two-dimensional 1H-NMR (nuclear magnetic resonance)…”
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Probing Copper super(2) super(+) Binding to the Prion Protein Using Diamagnetic Nickel super(2) super(+) and super(1)H NMR: The Unstructured N terminus Facilitates the Coordination of Six Copper super(2) super(+) Ions at Physiological Concentrations by Jones, CE, Klewpatinond, M, Abdelraheim, SR, Brown, DR, Viles, J H

“…The prion protein (PrP) is a Cu super(2) super(+) binding cell surface glyco-protein. Misfolding of PrP into a beta -sheet rich conformation is associated with…”
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