Behavioral and neurological evaluation of workers exposed to carbon disulfide (CS2) /

Mode of access: Internet.

Molybdenum; its ores and their concentration, with a discussion of markets, prices, and uses,

"Tabulation of molybdenite and of wulfenite occurrences in the United States": p. 86-90.

Tables of interplanar spacings computed for the characteristic radiations of copper, molybdenum, iron, chromium and cobalt

"ASTIA document no. AD142344."

Investigation of the fatigue properties of molybdenum under various conditions of temperature, coatings, and stress concentration

"Materials Central, Contract No. AF 33(616)-5915, Project No. 7350."

An investigation of the relationship of hot-hardness to the elevated temperature extrusion behavior of selected arc-cast molybdenum base alloys.

"Project no. 7351."

The mineral industry of the British Empire and foreign countries. Statistics, 1920-1922. Molybdenum.

At head of title: Imperial Mineral Resources Bureau.

The mineral industry of the British Empire and foreign countries. Statistics, 1919-1921. Molybdenum.

At head of title: Imperial Mineral Resources Bureau.

The mineral industry of the British Empire and foreign countries. War period. Molybdenum. (1913-1919)

At head of title: Imperial mineral resources bureau.

Arc-cast molybdenum and its alloys.

Cover title.

The molybdenum industry in New South Wales.

At head of title: New South Wales. Department of Mines.

Uber disulfide mit benachbarten doppelbindungen.

Thesis (doctoral)--

Uber Thiobenzoesauren und Disulfide mit benachbarten Doppelbindungen /

Thesis (doctoral)--Albert-Ludwigs-Universitat zu Freiburg im Breisgau, 1907.

Ueber Disulfide mit benachbarten Doppelbindungen /

Thesis (doctoral)--Albert-Ludwigs-Universitat zu Freiburg im Breisgau, 1908.

Disulfide folding pathways of cystine knot proteins: Tying the knot within the circular backbone of the cyclotides

The plant cyclotides are a fascinating family of circular proteins that contain a cyclic cystine knot motif. The knotted topology and cyclic nature of the cyclotides pose interesting questions about folding mechanisms and how the knotted arrangement of disulfide bonds is formed. In the current study we have examined the oxidative refolding and reductive unfolding of the prototypic cyclotide, kalata B1. A stable two-disulfide intermediate accumulated during oxidative refolding but not in reductive unfolding. Mass spectrometry and NMR spectroscopy were used to show that the intermediate contained a native-like structure with two native disulfide bonds topologically similar to the intermediate isolated for the related cystine knot protein EETI-II (LeNguyen, D., Heitz, A., Chiche, L., El Hajji, M., and Castro B. (1993) Protein Sci. 2, 165-174). However, the folding intermediate observed for kalata B1 is not the immediate precursor of the three-disulfide native peptide and does not accumulate in the reductive unfolding process, in contrast to the intermediate observed for EETI-II. These alternative pathways of linear and cyclic cystine knot proteins appear to be related to the constraints imposed by the cyclic backbone of kalata B1 and the different ring size of the cystine knot. The three-dimensional structure of a synthetic version of the two-disulfide intermediate of kalata B1 in which Ala residues replace the reduced Cys residues provides a structural insight into why the two-disulfide intermediate is a kinetic trap on the folding pathway.

Structure of Petunia hybrida Defensin 1, a Novel Plant Defensin with Five Disulfide Bonds

The structure of a novel plant defensin isolated from the flowers of Petunia hybrida has been determined by H-1 NMR spectroscopy. P. hybrida defensin 1 (PhD1) is a basic, cysteine-rich, antifungal protein of 47 residues and is the first example of a new subclass of plant defensins with five disulfide bonds whose structure has been determined. PhD1 has the fold of the cysteine-stabilized alphabeta motif, consisting of an alpha-helix and a triple-stranded antiparallel beta-sheet, except that it contains a fifth disulfide bond from the first loop to the alpha-helix. The additional disulfide bond is accommodated in PhD1 without any alteration of its tertiary structure with respect to other plant defensins. Comparison of its structure with those of classic, four-disulfide defensins has allowed us to identify a previously unrecognized hydrogen bond network that is integral to structure stabilization in the family.