36 research outputs found
Localized Character of 4f Electrons in CeRh(x=2,3) and CeNi(x=2,5)
We have measured Ce 4f spectral weights of extremely -like
Ce-transition metal intermetallic compounds CeRh (x=2,3) and CeNi
(x=2,5) by using the {\it bulk-sensitive} resonant photoemission technique at
the Ce ()-edge. Unprecedentedly high energy resolution and
longer escape depth of photoemitted electron at this photon energy enabled us
to distinguish the sharp Kondo resonance tails at the Fermi level, which can be
well described by the Gunnarsson-Sch\"onhammer(GS) calculation based on the
Anderson Impurity Hamiltonian. On the other hand, the itinerant 4f band
description shows big discrepancies, which implies that Ce 4f electrons retain
localized characters even in extremely -like compounds.Comment: 4 pages, 3 figures, submitted to Phys. Rev. Let
Faithful chaperones
This review describes the properties of some rare eukaryotic chaperones that each assist in the folding of only one target protein. In particular, we describe (1) the tubulin cofactors, (2) p47, which assists in the folding of collagen, (3) α-hemoglobin stabilizing protein (AHSP), (4) the adenovirus L4-100 K protein, which is a chaperone of the major structural viral protein, hexon, and (5) HYPK, the huntingtin-interacting protein. These various-sized proteins (102–1,190 amino acids long) are all involved in the folding of oligomeric polypeptides but are otherwise functionally unique, as they each assist only one particular client. This raises a question regarding the biosynthetic cost of the high-level production of such chaperones. As the clients of faithful chaperones are all abundant proteins that are essential cellular or viral components, it is conceivable that this necessary metabolic expenditure withstood evolutionary pressure to minimize biosynthetic costs. Nevertheless, the complexity of the folding pathways in which these chaperones are involved results in error-prone processes. Several human disorders associated with these chaperones are discussed