Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI

Piergiorgio Percipalle; Sandor Pongor; Sotir Zakhariev; Corrado Guarnaccia; Rosaria Saletti; Salvatore Foti; Salvatore Fisichella

doi:10.1255/ejms.33

Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI

Piergiorgio Percipalle, Sandor Pongor, Sotir Zakhariev, Corrado Guarnaccia, Rosaria Saletti, Salvatore Foti, Salvatore Fisichella

Biology

Research output: Contribution to journal › Article › peer-review

Abstract

The synthesis and structural characterisation of the 1-63 N-terminal (Nter) sequence of the cI434 repressor is described. Matrix assisted laser desorption ionisation mass spectrometry of the intact peptide yielded a molecular weight determination of 6897.4, with respect to a calculated value of 6891.9. The correctness of the sequence was substantiated by fast atom bombardment mass spectrometric identification of complementary peptide fragments obtained by tryptic and chymotrypic digestion and partial separation by reversed-phase high-performance liquid chromatography. The results show the potential of this approach for characterising high molecular weight synthetic peptides.

Original language	English (US)
Pages (from-to)	151-159
Number of pages	9
Journal	European Journal of Mass Spectrometry
Volume	3
Issue number	2
DOIs	https://doi.org/10.1255/ejms.33
State	Published - 1997

Keywords

434 repressor cI
DNA-binding proteins
Fast atom bombardment
Mass spectrometry
Matrix assisted laser desorption ionisation
Structural characterisation
Synthetic model peptides
Tryptic and chymotryptic cleavages

ASJC Scopus subject areas

Atomic and Molecular Physics, and Optics
Spectroscopy

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10.1255/ejms.33

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title = "Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI",

abstract = "The synthesis and structural characterisation of the 1-63 N-terminal (Nter) sequence of the cI434 repressor is described. Matrix assisted laser desorption ionisation mass spectrometry of the intact peptide yielded a molecular weight determination of 6897.4, with respect to a calculated value of 6891.9. The correctness of the sequence was substantiated by fast atom bombardment mass spectrometric identification of complementary peptide fragments obtained by tryptic and chymotrypic digestion and partial separation by reversed-phase high-performance liquid chromatography. The results show the potential of this approach for characterising high molecular weight synthetic peptides.",

keywords = "434 repressor cI, DNA-binding proteins, Fast atom bombardment, Mass spectrometry, Matrix assisted laser desorption ionisation, Structural characterisation, Synthetic model peptides, Tryptic and chymotryptic cleavages",

author = "Piergiorgio Percipalle and Sandor Pongor and Sotir Zakhariev and Corrado Guarnaccia and Rosaria Saletti and Salvatore Foti and Salvatore Fisichella",

year = "1997",

doi = "10.1255/ejms.33",

language = "English (US)",

volume = "3",

pages = "151--159",

journal = "European Journal of Mass Spectrometry",

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T1 - Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI

AU - Percipalle, Piergiorgio

AU - Pongor, Sandor

AU - Zakhariev, Sotir

AU - Guarnaccia, Corrado

AU - Saletti, Rosaria

AU - Foti, Salvatore

AU - Fisichella, Salvatore

PY - 1997

Y1 - 1997

N2 - The synthesis and structural characterisation of the 1-63 N-terminal (Nter) sequence of the cI434 repressor is described. Matrix assisted laser desorption ionisation mass spectrometry of the intact peptide yielded a molecular weight determination of 6897.4, with respect to a calculated value of 6891.9. The correctness of the sequence was substantiated by fast atom bombardment mass spectrometric identification of complementary peptide fragments obtained by tryptic and chymotrypic digestion and partial separation by reversed-phase high-performance liquid chromatography. The results show the potential of this approach for characterising high molecular weight synthetic peptides.

AB - The synthesis and structural characterisation of the 1-63 N-terminal (Nter) sequence of the cI434 repressor is described. Matrix assisted laser desorption ionisation mass spectrometry of the intact peptide yielded a molecular weight determination of 6897.4, with respect to a calculated value of 6891.9. The correctness of the sequence was substantiated by fast atom bombardment mass spectrometric identification of complementary peptide fragments obtained by tryptic and chymotrypic digestion and partial separation by reversed-phase high-performance liquid chromatography. The results show the potential of this approach for characterising high molecular weight synthetic peptides.

KW - 434 repressor cI

KW - DNA-binding proteins

KW - Fast atom bombardment

KW - Mass spectrometry

KW - Matrix assisted laser desorption ionisation

KW - Structural characterisation

KW - Synthetic model peptides

KW - Tryptic and chymotryptic cleavages

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DO - 10.1255/ejms.33

M3 - Article

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SN - 1469-0667

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JO - European Journal of Mass Spectrometry

JF - European Journal of Mass Spectrometry

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Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI

Abstract

Keywords

ASJC Scopus subject areas

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