related to degree

• Strable, Erica, Ph.D. in Biochemistry, Scripps Research 2000 - 2006

authors

• Meunier, S.
• Strable, Erica
• Finn, M.G.

publication date

• 2004

journal

• Chemistry & Biology  Journal

abstract

• Cowpea mosaic virus is composed of 60 identical copies of a two-subunit protein organized in pentameric assemblies around the icosahedral 5-fold symmetry axis. Treatment of the virus with the Ni(II) complex of the tripeptide GGH and a peroxide oxidant, or irradiation in the presence of Ru(bpy)(3)(2+) and persulfate generates covalent crosslinks across the pentameric subunit boundaries, effectively stitching the subunits together. Intersubunit crosslinking was found to occur exclusively at adjacent tyrosine residues (Y52-Y103), as predicted from the X-ray crystal structure of the capsid, and to be more extensive with the photochemical ruthenium system. The Ni/GGH oxidative procedure was also used to make covalent attachments to the virion by trapping with a functionalized disulfide reagent.

subject areas

• Capsid Proteins
• Comovirus
• Cross-Linking Reagents
• Crystallography, X-Ray
• Cysteine
• Hydrogen-Ion Concentration
• Models, Molecular
• Molecular Structure
• Mutation
• Nickel
• Oxidation-Reduction
• Peptides
• Photochemistry
• Phthalic Acids
• Protein Structure, Quaternary
• Ruthenium
• Spectrum Analysis
• Temperature
• Tyrosine
• Virion

International Standard Serial Number (ISSN)

• 1074-5521

Digital Object Identifier (DOI)

• 10.1016/j.chembiol.2004.02.019

PubMed ID

• 15123261

start page

• 319

end page

• 326

volume

• 11

issue

• 3