... assembly (CIA) machinery Dre2 EPR Mössbauer spectroscopy mutagenesis spectroscopy Iron–sulfur (Fe–S) cluster-containing proteins are ubiquitously found in all kingdoms of life [ 1 ]. Due to the intrinsic property of Fe–S clusters to accept or donate electrons, Fe–S proteins are involved...

...) crystallin spectroscopy stability The transparency and refractive power of the vertebrate eye lens is achieved by the high concentration and regular spatial distribution of crystallin proteins [ 1 , 2 ]. In the low protein turnover environment of the lens, transparency is maintained...

...- and chain-length dependent. CD indicates that Cu 2+ initially fills the site at His 111 within the PrP-(90–126) fragment. The pH-dependence of the Cu 2+ co-ordination is studied using EPR, visible CD and absorption spectroscopy. We present evidence that, at low pH (5.5) and sub-stoichiometric amounts of Cu...

... was estimated to adopt a folded conformation in water, as evidenced by CD spectroscopy. This was consistent with smaller, but still significant, downfield shifts of C α H protons relative to random-coil values. A second peptide was designed with two disulphide bonds to further constrain the peptide backbone...

... and characterized. The Y48K mutant is the only one that exhibits a significant increase of +117mV in redox potential compared with the wild-type protein while still supporting oxidative phosphorylation in vivo . Low temperature difference spectroscopy confirmed the formation of the holoprotein, while adsorption...

[email protected] ). 12 7 2000 25 10 2000 20 11 2000 The Biochemical Society, London © 2001 2001 Hofmeister salts small heat-shock protein spectroscopy Biochem. J. (2001) 354, 79 87 (Printed in Great Britain) 79 The molecular chaperone a-crystallin is in kinetic competition...