Paul D. Barker

TL;DR: An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions, challenging the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces.

TL;DR: This work has fused the sequence of the small, soluble cytochrome b562 to an SH3 dimer sequence that can form classical amyloid fibrils rapidly under well-defined conditions and binds metalloporphyrins, at half of the porphyrin binding sites as shown by UV-vis and NMR spectroscopies.

TL;DR: C-Type cytochromes are a group of proteins with diverse structures and functions and their common feature is covalent attachment of haem to one or more CXXCH motifs.

TL;DR: The solution structure of the oxidized, paramagnetic form of cytochrome b562 from Escherichia coli is reported as obtained from 1653 meaningful NOEs, and the pKa values affecting the hyperfine-shifted signals are discussed.

TL;DR: A new approach was developed to overproduce 15N-enriched yeast iso-1-cytochrome c in the periplasm of Escherichia coli to perform a study of the motions in the ms-micros time scale on the oxidized and reduced forms through rotating frame 15N relaxation rates and proton/deuterium exchange studies.