Localization of the membrane-associated region of vesicular stomatitis virus M protein at the N terminus, using the hydrophobic, photoreactive probe 125I-TID.

Abstract	The membrane-reactive, photoactivatable probe 125I-TID [3-(trifluoromethyl)-3-(m-[125I]iodophenyl)-3H-diazirine] was found to label the M protein of vesicular stomatitis virus about 40% as much as G protein in intact virions, in agreement with labeling studies with other probes. By analyzing limited tryptic digestion and specific chemical cleavage products, the label was essentially entirely localized within the first 19, and probably within the first 5 to 10, amino acid residues at the N terminus, identifying this short amphipathic segment as the likely site of interaction of M protein with the viral bilayer.
Authors	J Lenard, R Vanderoef
Journal	Journal of virology (J Virol) Vol. 64 Issue 7 Pg. 3486-91 (Jul 1990) ISSN: 0022-538X [Print] United States
PMID	2161951 (Publication Type: Journal Article)
Chemical References	Azirines Formates Membrane Proteins Viral Matrix Proteins formic acid 3-(trifluoromethyl)-3-(3-iodophenyl)diazirine Trypsin
Topics	Amino Acid Sequence Animals Azirines Binding Sites Cricetinae Formates Membrane Proteins (ultrastructure) Molecular Sequence Data Peptide Mapping Photochemistry Solubility Trypsin Vesicular stomatitis Indiana virus (ultrastructure) Viral Matrix Proteins (ultrastructure)

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