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In Situ Spatial Organization of Potato Virus A Coat Protein Subunits as Assessed by Tritium Bombardment
This is the first model of the three-dimensional structure of a potyvirus coat protein, derived from the experimental data obtained by tritium bombardment combined with predictions of secondary-structure elements and the principles of packing α-helices and β-structures in proteins. Expand
Dysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation.
It is reported that TMV movement protein (MP)-specific protein kinases (PKs) associated with the ER of tobacco were capable of phosphorylating Thr(104) in TMV MP. Expand
Intracellular serine protease of Bacillus subtilis: sequence homology with extracellular subtilisins.
The occurrence of two homologous genes in the cell might accelerate the evolution of serine protease not only by the loosening of selective constrainst, but also by creation of sequence variants by means of intragenic recombination. Expand
Prediction of arenavirus fusion peptides on the basis of computer analysis of envelope protein sequences
Two regions of GP2 surface protein from 5 viruses of Arenaviridae family have been detected with properties typical of fusion peptides of other enveloped viruses. Expand
Partial N‐terminal amino acid sequences of polypeptides p14 and p12 of encephalomyocarditis virus are identical and correspond to the N‐terminus of the viral polyprotein
The single initiation site operating in the translation system corresponds to the start of the polyprotein molecule as well as the N‐terminus of EMC virus polyprotein sequence deduced from the primary structure of the viral genome. Expand
Direct comparison of the subtilisin-like intracellular protease of Bacillus licheniformis with the homologous enzymes of Bacillus subtilis.
Intracellular serine proteases of Bacillus licheniformis and Bacillus subtilis are closely related and have shown the ability to cleaveopolysaccharide from E.coli to form polypeptide. Expand
Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50.
Intracellular serine proteinase was isolated from sporulating cells of Bacillus subtilis Marburg 168 by gramicidin S-Sepharose 4B affinity chromatography. The enzymological characteristics, the aminoExpand
The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment.
Intact influenza A virions were bombarded with thermally activated tritium atoms, and the intramolecular distribution of the label in the matrix protein M1 was analyzed to determine the in situ accessibility of its tryptic fragments to propose a model of M1 arrangement in the virus particle. Expand
S Acylation of the Hemagglutinin of Influenza Viruses: Mass Spectrometry Reveals Site-Specific Attachment of Stearic Acid to a Transmembrane Cysteine
MS analysis of recombinant viruses with deletions of individual cysteines, as well as tandem-MS sequencing, revealed the surprising result that stearate is exclusively attached to the cysteine positioned in the transmembrane region of HA. Expand
The use of thermally activated tritium atoms for structural-biological investigations: the topography of the TMV protein-accessible surface of the virus.
The accessibility profile of amino acid residues in a protein polypeptide chain was determined from data on the intramolecular distribution of a tritium label in the TMV protein, and it was shown that tryptic peptides T3, T4, T12, the N-terminal region of peptide T1 and the proximal tryptic protein T8 are accessible totritium labelling. Expand