Novel Peptide Dissociation:  Gas-Phase Intramolecular Rearrangement of Internal Amino Acid Residues

1997 ◽  
Vol 119 (24) ◽  
pp. 5481-5488 ◽  
Author(s):  
Richard W. Vachet ◽  
Barney M. Bishop ◽  
Bruce W. Erickson ◽  
Gary L. Glish
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Intramolecular Rearrangement ◽  
Amino Acid Residues ◽  
Peptide Dissociation

scholarly journals Amino acid sequence of versutoxin, a lethal neurotoxin from the venom of the funnel-web spider Atrax versutus

1988 ◽  
Vol 250 (2) ◽  
pp. 401-405 ◽  
Author(s):  
M R Brown ◽  
D D Sheumack ◽  
M I Tyler ◽  
M E H Howden
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gas Phase ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Single Chain ◽  
Male And Female ◽  
Web Spider ◽  
Phase Protein ◽  
Protein Sequencer

The complete amino acid sequence of versutoxin, a lethal neurotoxic polypeptide isolated from the venom of male and female funnel-web spiders of the species Atrax versutus, was determined. Sequencing was performed in a gas-phase protein sequencer by automated Edman degradation of the S-carboxymethylated toxin and fragments of it produced by reaction with CNBr. Versutoxin consisted of a single chain of 42 amino acid residues. It was found to have a high proportion of basic residues and of cystine. The primary structure showed marked homology with that of robustoxin, a novel neurotoxin recently isolated from the venom of another funnel-web-spider species, Atrax robustus.

Volumes of Individual Amino Acid Residues in Gas-Phase Peptide Ions

1999 ◽  
Vol 121 (16) ◽  
pp. 4031-4039 ◽  
Author(s):  
Anne E. Counterman ◽  
David E. Clemmer
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Individual Amino Acid ◽  
Amino Acid Residues ◽  
Peptide Ions

scholarly journals Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking

2021 ◽  
Author(s):  
Melanie Cheung See Kit ◽  
Veronica V. Carvalho ◽  
Jonah Z. Vilseck ◽  
Ian Webb
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Gas Phase ◽  
Structural Changes ◽  
Cross Linking ◽  
Distance Constraint ◽  
Amino Acid Residues ◽  
Ion Chemistry ◽  
Specific Chemical ◽  
Gas Phase Ion

Intramolecular interactions within a protein are key in maintaining protein tertiary structure and understanding how proteins function. Ion mobility-mass spectrometry (IM-MS) has become a widely used approach in structural biology since it provides rapid measurements of collision cross sections (CCS), which inform on the gas-phase conformation of the biomolecule under study. Gas-phase ion/ion reactions target amino acid residues with specific chemical properties and the modified sites can be identified by MS. In this study, electrostatically reactive, gas-phase ion/ion chemistry and IM-MS are combined to characterize the structural changes between ubiquitin electrosprayed from aqueous and denaturing conditions. The electrostatic attachment of sulfo-NHS acetate to ubiquitin via ion/ion reactions and fragmentation by electron-capture dissociation (ECD) provide the identification of the most accessible protonated sites within ubiquitin as the sulfonate group forms an electrostatic complex with accessible protonated side chains. The protonated sites identified by ECD from the different solution conditions are distinct and, in some cases, reflect the disruption of interactions such as salt bridges that maintain the native protein structure. This agrees with previously published literature demonstrating that a high methanol concentration at low pH causes the structure of ubiquitin to change from a native (N) state to a more elongated A state. Results using gas-phase, electrostatic cross-linking reagents also point to similar structural changes and further confirm the role of methanol and acid in favoring a more unfolded conformation. Since cross-linking reagents have a distance constraint for the two reactive sites, the data is valuable in guiding computational structures generated by molecular dynamics. The research presented here describes a promising strategy that can detect subtle changes in the local environment of targeted amino acid residues to inform on changes in the overall protein structure.

Identification of Phosphorylated Amino Acid Residues During Gas Phase Sequencing

1987 ◽  
pp. 479-482
Author(s):  
Yuhuan Wang ◽  
Alexander W. Bell ◽  
Mark A. Hermodson ◽  
Peter J. Roach
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Amino Acid Residues ◽  
Phosphorylated Amino Acid

scholarly journals Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking

2020 ◽  
Author(s):  
Melanie Cheung See Kit ◽  
Veronica V. Carvalho ◽  
Jonah Z. Vilsek ◽  
Ian Webb
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Gas Phase ◽  
Structural Changes ◽  
Cross Linking ◽  
Distance Constraint ◽  
Amino Acid Residues ◽  
Ion Chemistry ◽  
Specific Chemical ◽  
Gas Phase Ion

Intramolecular interactions within a protein are key in maintaining protein tertiary structure and understanding how proteins function. Ion mobility-mass spectrometry (IM-MS) has become a widely used approach in structural biology since it provides rapid measurements of collision cross sections (CCS), which inform on the gas-phase conformation of the biomolecule under study. Gas-phase ion/ion reactions target amino acid residues with specific chemical properties and the modified sites can be identified by MS. In this study, electrostatically reactive, gas-phase ion/ion chemistry and IM-MS are combined to characterize the structural changes between ubiquitin electrosprayed from aqueous and denaturing conditions. The electrostatic attachment of sulfo-NHS acetate to ubiquitin via ion/ion reactions and fragmentation by electron-capture dissociation (ECD) provide the identification of the most accessible protonated sites within ubiquitin as the sulfonate group forms an electrostatic complex with accessible protonated side chains. The protonated sites identified by ECD from the different solution conditions are distinct and, in some cases, reflect the disruption of interactions such as salt bridges that maintain the native protein structure. This agrees with previously published literature demonstrating that a high methanol concentration at low pH causes the structure of ubiquitin to change from a native (N) state to a more elongated A state. Results using gas-phase, electrostatic cross-linking reagents also point to similar structural changes and further confirm the role of methanol and acid in favoring a more unfolded conformation. Since cross-linking reagents have a distance constraint for the two reactive sites, the data is valuable in guiding computational structures generated by molecular dynamics. The research presented here describes a promising strategy that can detect subtle changes in the local environment of targeted amino acid residues to inform on changes in the overall protein structure.

scholarly journals Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking

2020 ◽  
Author(s):  
Melanie Cheung See Kit ◽  
Veronica V. Carvalho ◽  
Jonah Z. Vilsek ◽  
Ian Webb
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Gas Phase ◽  
Structural Changes ◽  
Cross Linking ◽  
Distance Constraint ◽  
Amino Acid Residues ◽  
Ion Chemistry ◽  
Specific Chemical ◽  
Gas Phase Ion

Intramolecular interactions within a protein are key in maintaining protein tertiary structure and understanding how proteins function. Ion mobility-mass spectrometry (IM-MS) has become a widely used approach in structural biology since it provides rapid measurements of collision cross sections (CCS), which inform on the gas-phase conformation of the biomolecule under study. Gas-phase ion/ion reactions target amino acid residues with specific chemical properties and the modified sites can be identified by MS. In this study, electrostatically reactive, gas-phase ion/ion chemistry and IM-MS are combined to characterize the structural changes between ubiquitin electrosprayed from aqueous and denaturing conditions. The electrostatic attachment of sulfo-NHS acetate to ubiquitin via ion/ion reactions and fragmentation by electron-capture dissociation (ECD) provide the identification of the most accessible protonated sites within ubiquitin as the sulfonate group forms an electrostatic complex with accessible protonated side chains. The protonated sites identified by ECD from the different solution conditions are distinct and, in some cases, reflect the disruption of interactions such as salt bridges that maintain the native protein structure. This agrees with previously published literature demonstrating that a high methanol concentration at low pH causes the structure of ubiquitin to change from a native (N) state to a more elongated A state. Results using gas-phase, electrostatic cross-linking reagents also point to similar structural changes and further confirm the role of methanol and acid in favoring a more unfolded conformation. Since cross-linking reagents have a distance constraint for the two reactive sites, the data is valuable in guiding computational structures generated by molecular dynamics. The research presented here describes a promising strategy that can detect subtle changes in the local environment of targeted amino acid residues to inform on changes in the overall protein structure.

Sign in / Sign up

Export Citation Format

Share Document