Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Philip K. Hammen"'
Publikováno v:
Protein Science. 4:936-944
Anomalous NMR behavior of the hydroxyl proton resonance for Ser 31 has been reported for histidine-containing protein (HPr) from two microorganisms: Escherichia coli and Staphylococcus aureus. The unusual slow exchange and chemical shift exhibited by
Publikováno v:
Protein Science. 11:1026-1035
Most mitochondrial matrix space proteins are synthesized as a precursor protein, and the N-terminal extension of amino acids that served as the leader sequence is removed after import by the action of a metalloprotease called mitochondrial processing
Autor:
Henry Weiner, Philip K. Hammen
Publikováno v:
FEBS Letters. 468:101-104
TOM5 is a small outer mitochondrial membrane protein in Saccharomyces cerevisiae and is part of a multi-protein translocator complex, which mediates protein import into mitochondria. Presently, nothing is known about the conformational preferences of
Autor:
Philip K. Hammen, Henry Weiner
Publikováno v:
The Journal of Experimental Zoology. 282:280-283
While having essentially no amino acid sequence homology, the mitochondrial leader sequences of different pre-proteins carry out the same function of targeting the protein to mitochondria. Among the common attributes that have been noted for leader s
Publikováno v:
Biochemistry. 33:8610-8617
The N-terminal sequences of rhodanese and 3-oxoacyl-CoA thiolase, two mitochondrial matrix proteins that are not proteolytically processed upon import, have been studied by NMR and CD spectroscopy. In aqueous trifluoroethanol, in the presence of mice
Publikováno v:
Biochemistry. 30:11842-11850
Analysis of the histidine-containing protein (HPr) from Escherichia coli by two-dimensional homonuclear and heteronuclear nuclear magnetic resonance techniques has been performed, extending the work originally reported [Klevit, R. E., Drobny, G. D.,
Autor:
Philip K. Hammen, Niels H. Andersen
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 1:263-266
Unlike natural GnRH (which shows a random flexible conformation with a populated reverse turn at residues 3,4), napharelin adopts (in aqueous media containing hexafluoroisopropanol) a non-random conformation in the region of the putative pharmacophor
Publikováno v:
The Journal of biological chemistry. 278(16)
Proteins destined for the mitochondrial matrix space have leader sequences that are typically present at the most N-terminal end of the nuclear-encoded precursor protein. The leaders are rich in positive charges and usually deficient of negative char
Publikováno v:
Biochemistry. 41(22)
Crystallographic analysis revealed that the nicotinamide ring of NAD can bind with multiconformations to aldehyde dehydrogenase (ALDH) (Ni, L., Zhou, J., Hurley, T. D., and Weiner, H. (1999) Protein Sci. 8, 2784-2790). Electron densities can be defin
Autor:
Larry L. Murdock, Philip K. Hammen, Ray A. Bressan, Ron A. Salzman, Keyan Zhu-Salzman, Paul M. Hasegawa, Hisashi Koiwa
Publikováno v:
Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 132(2)
Site-directed mutagenesis previously identified the residues responsible for the biological activity of the plant defense legume lectin, Griffonia simplicifolia lectin II (GSII) [Proc. Natl. Acad. Sci. USA 95, (1998) 15123-15128]. However, these resu