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In vivo phosphorylation site of hexokinase 2 in Saccharomyces cerevisiae.
TLDR
The principal and perhaps sole site of phosphorylation is now identified as residue serine-15, by observation of a single tryptic peptide difference, its sequencing and size determination by mass spectrometry, and by mutation to alanine, which prevents phosphorylated in vivo.
Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes.
TLDR
Point mutations in the cSH2 domain located at the interface with the peptide were sufficient to constitutively activate PLC-γ1, suggesting that peptide engagement directly interferes with the capacity of the c SH2 domain to block the lipase active site.
Autophosphorylation-inactivation site of hexokinase 2 in Saccharomyces cerevisiae.
TLDR
The site of inactivation by autophosphorylation as serine-158 is identified by observation of a single tryptic peptide difference, peptide sequencing, and size determination by mass spectrometry.
Purification and characterization of colicin V from Escherichia coli culture supernatants.
TLDR
The purification scheme provides a rapid and simple way to obtain ColV for further biochemical analysis, and shows that it has a mass consistent with the mass of the unmodified 88 amino acid polypeptide.
Photoaffinity labeling of the Klenow fragment with 8-azido-dATP.
Rapid purification of overexpressed T4 DNA polymerase.
TLDR
A method for purifying T4 DNA polymerase from cells harboring overexpression plasmids is described and consistently provides enzyme preparations which are at least 98% pure.
Memory and Perfection in Ferroelastic Inclusion Compounds
In a series of ferroelastic urea inclusion compounds (UICs), in which domain reorientation occurs upon application of an external anisotropic force, introduction of a relaxive impurity that disrupts
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