Protein conformation in bacterial spinae

Coombs, Robert W.; Verpoorte, Jacob A.; Easterbrook, K. B.

doi:10.1002/bip.1976.360151204

Cited by 17 publications

(1 citation statement)

References 30 publications

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“…A small enhancement of secondary structure by detergents is not unusual but does suggest that the association with membrane lipid or other hydrophobic protein may also enhance the degree of secondary structure. These properties are very similar to the outer membrane porins of Escherichia coli (Rosenbusch, 1974) and the surface spinae of a marine pseudomonad (Coombs et al, 1976). Other membrane-imbedded proteins and peptides normally exhibit increased a-helical content upon association with phospholipids (Hammer & Schullery, 1970;Cockle et al, 1978;Shirahama & Yang, 1979), but these are generally characterized by long spans of a helix (Wallace, 1982).…”

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confidence: 92%

Purification and characterization of the cell surface virulent A protein from Aeromonas salmonicida

Phipps¹,

Trust²,

Ishiguro³

et al. 1983

Biochemistry

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The predominant cell surface protein (A protein) of Aeromonas salmonicida has been purified in high yield from outer membranes by using a combination of detergent and chaotropic extraction methods as well as exclusion and ion-exchange chromatography. The A protein was primarily monomeric, Mr 50 000, but readily formed oligomers at high protein or low salt concentrations. Several isoelectric forms were distinguishable with purified protein as well as in situ on the cell surface. Neither phosphate nor carbohydrate was detectable. The A protein was hydrophobic in composition and the N-terminal sequence highly hydrophobic. From CD spectra the A protein exhibited 14% alpha helix and 19-28% beta structure and could also be readily crystallized. By fluorescent antibody staining the A protein was shown to cover the entire cell surface but was absent from A protein deficient mutants. This protein appears to have no apparent enzymatic activity but rather constitutes a macromolecular refractile protein barrier essential for virulence.

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mentioning

confidence: 92%

Purification and characterization of the cell surface virulent A protein from Aeromonas salmonicida

Phipps¹,

Trust²,

Ishiguro³

et al. 1983

Biochemistry

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Monitoring of solid phase peptide synthesis by FT-IR spectroscopy

Henkel

Bayer

1998

J. Peptide Sci.

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Aggregation phenomena of growing peptides on the resin have seldom been investigated. We report here how conformations are determined by FT-IR spectroscopy. Therefore the sequence 80-99 of HIV 1-protease was synthesized. After every coupling a resin sample was taken out of the reaction column and a FT-IR spectrum recorded. The results were compared with the UV monitoring obtained from another synthesis of the same peptide.

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Secondary structural analysis of retrovirus integrase: Characterization by circular dichroism and empirical prediction methods

et al. 1989

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The retrovirus integrase (IN) protein is essential for integration of viral DNA into host DNA. The secondary structure of the purified IN protein from avian myeloblastosis virus was investigated by both circular dichroism (CD) spectroscopy and five empirical prediction methods. The secondary structures determined from the resolving of CD spectra through a least-squares curve fitting procedure were compared with those predicted from four statistical methods, e.g., the Chou-Fasman, Garnier-Osguthorpe-Robson, Nishikawa-Ooi, and a JOINT scheme which combined all three of these methods, plus a pure a priori one, the Ptitsyn-Finkelstein method. Among all of the methods used, the Nishikawa-Ooi prediction gave the closest match in the composition of secondary structure to the CD result, although the other methods each correctly predicted one or more secondary structural group. Most of the alpha-helix and beta-sheet states predicted by the Ptitsyn-Finkelstein method were in accord with the Nishikawa-Ooi method. Secondary structural predictions by the Nishikawa-Ooi method were extended further to include IN proteins from four phylogenetic distinct retroviruses. The structural relationships between the four most conserved amino acid blocks of these IN proteins were compared using sequence homology and secondary structure predictions.

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Protein conformation in bacterial spinae

Cited by 17 publications

References 30 publications

Purification and characterization of the cell surface virulent A protein from Aeromonas salmonicida

Purification and characterization of the cell surface virulent A protein from Aeromonas salmonicida

Monitoring of solid phase peptide synthesis by FT-IR spectroscopy

Secondary structural analysis of retrovirus integrase: Characterization by circular dichroism and empirical prediction methods

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