Publications by Dr. John Viles
Probing copper2+ binding to the prion protein using
diamagnetic nickel2+ and 1H NMR: The unstructured N-terminus facilitates
the coordination of six Cu2+ ions at physiological concentrations.
Preferential copper2+ coordination by His96 and His111
induces ?-sheet formation in the unstructured amyloidogenic region
of the prion protein.
Copper binding to the amyloid-beta (A?) peptide associated
with Alzheimer’s disease.
Copper binding to the octarepeats of the prion protein.
Affinity, specificity, folding, and cooperativity: insights from circular
Potential bias in NMR relaxation data introduced
by peak intensity analysis and curve fitting methods.
Local structural plasticity of the prion protein.
Analysis of NMR relaxation dynamics.
Copper binding to the prion protein: structural implications
of four identical cooperative binding sites.
Design, synthesis and structure of a zinc finger
with an artificial beta-turn.
Structure of the recombinant full-length hamster
prion protein PrP(29-231): the N terminus is highly flexible.
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.
Observation of albumin resonances in proton nuclear
magnetic resonance spectra of human blood plasma: N-terminal assignments
aided by use of modified recombinant albumin.
Solution structure of a biologically active cyclic
LDV peptide analogue containing a type II' beta-turn mimetic.
Towards meeting the Paracelsus Challenge: The design,
synthesis, and characterization of paracelsin-43, an alpha-helical
protein with over 50% sequence identity to an all-beta protein.
Involvement of a lysine residue in the N-terminal
Ni2+ and Cu2+ binding site of serum albumins. Comparison with Co2+,
Cd2+ and Al3+.