A method for determining an amino acid sequence of a polypeptide, including comprising: contacting a first sample containing the polypeptide with a first protease (e.g., Trypsin) to produce a first set of digested peptide fragments; fragmenting the first set of digested peptide fragments to produce a first set of fragmented peptide ions; determining masses of the first set of fragmented peptide ions; contacting a second sample containing the polypeptide with a second protease (e.g., Tryp-N); fragmenting the second set of digested peptide fragments to produce a second set of fragmented peptide ions; selecting pairs of peptide ions from the first and the second set of fragmented peptide ions that differ in mass by a mass of an arginine amino acid residue or a lysine amino acid residue; assigning an ion type (either N-terminal peptide ion or C-terminal peptide ion) to the selected pairs of the peptide ions from two sets of fragmented peptide ions; selecting a mass ladder of the same-type peptide ions in either set of fragmented peptide ions with incremental mass by the mass of amino acid residue(s), and assembling the identified amino acid residues from the mass ladder to determine the amino acid sequence of the polypeptide of interest.

A method for determining an amino acid sequence of a polypeptide, including comprising: contacting a first sample containing the polypeptide with a first protease(e.g., Trypsin) to produce a first set of digested peptide fragments; fragmenting the first set of digested peptide fragments to produce a first set of fragmented peptide ions; determining masses of the first set of fragmented peptide ions; contacting a second sample containing the polypeptide with a second protease (e.g., Tryp-N); fragmenting the second set of digested peptide fragments to produce a second set of fragmented peptide ions; selecting pairs of peptide ions from the first and the second set of fragmented peptide ions that differ in mass by a mass of an arginine amino acid residue or a lysine amino acid residue; assigning an ion type (either N-terminal peptide ion or C-terminal peptide ion) to the selected pairs of the peptide ions from two sets of fragmented peptide ions;selecting a mass ladder of the same-type peptide ions in either set of fragmented peptide ions with incremental mass by the mass of amino acid residue(s), and assembling the identified amino acid residues from the mass ladder to determine the amino acid sequence of the polypeptide of interest.

An accelerator mass spectrometry system for measuring an isotopic ratio of a chemical element in a sample. The system includes an ion source generating a beam of negative ions of the chemical element containing ions of first and second isotopes of the chemical element, a first analyzer section, comprising a first mass analyzer; a tandem accelerator comprising a first accelerating section, a charge stripping section for converting the negative ions into positive ions, and a second accelerating section behind the charge stripping section. A second analyzer section includes a second mass analyzer and an electrostatic analyzer; a particle detector; and a controller system configured to control the first mass analyzer section and the second analyzer section such that the ions of the first and second isotopes traverse the tandem accelerator and ions of only one of the first and second isotopes enter the particle detector. An additional analyzer is located in between the charge stripping section and the second accelerating section and is configured to receive positive ions that have exited the charge stripping section and to separate positive ions having a charge state corresponding to a predetermined charge-state value from positive ions having a charge state not corresponding to the predetermined charge-state value, so as to transmit ions with different charge states in mutually different directions such that only ions having a charge state corresponding to the predetermined charge-state value are transmitted towards the particle detector.

A method for determining an amino acid sequence of a polypeptide, including comprising: contacting a first sample containing the polypeptide with a first protease(e.g., Trypsin) to produce a first set of digested peptide fragments; fragmenting the first set of digested peptide fragments to produce a first set of fragmented peptide ions; determining masses of the first set of fragmented peptide ions; contacting a second sample containing the polypeptide with a second protease (e.g., Tryp-N); fragmenting the second set of digested peptide fragments to produce a second set of fragmented peptide ions; selecting pairs of peptide ions from the first and the second set of fragmented peptide ions that differ in mass by a mass of an arginine amino acid residue or a lysine amino acid residue; assigning an ion type (either N-terminal peptide ion or C-terminal peptide ion) to the selected pairs of the peptide ions from two sets of fragmented peptide ions;selecting a mass ladder of the same-type peptide ions in either set of fragmented peptide ions with incremental mass by the mass of amino acid residue(s), and assembling the identified amino acid residues from the mass ladder to determine the amino acid sequence of the polypeptide of interest.

An accelerator mass spectrometry system for measuring an isotopic ratio of a chemical element in a sample. The system includes an ion source generating a beam of negative ions of the chemical element containing ions of first and second isotopes of the chemical element, a first analyzer section, comprising a first mass analyzer; a tandem accelerator comprising a first accelerating section, a charge stripping section for converting the negative ions into positive ions, and a second accelerating section behind the charge stripping section. A second analyzer section includes a second mass analyzer and an electrostatic analyzer; a particle detector; and a controller system configured to control the first mass analyzer section and the second analyzer section such that the ions of the first and second isotopes traverse the tandem accelerator and ions of only one of the first and second isotopes enter the particle detector. An additional analyzer is located in between the charge stripping section and the second accelerating section and is configured to receive positive ions that have exited the charge stripping section and to separate positive ions having a charge state corresponding to a predetermined charge-state value from positive ions having a charge state not corresponding to the predetermined charge-state value, so as to transmit ions with different charge states in mutually different directions such that only ions having a charge state corresponding to the predetermined charge-state value are transmitted towards the particle detector.

A method for determining an amino acid sequence of a polypeptide, including comprising: contacting a first sample containing the polypeptide with a first protease (e.g., Trypsin) to produce a first set of digested peptide fragments; fragmenting the first set of digested peptide fragments to produce a first set of fragmented peptide ions; determining masses of the first set of fragmented peptide ions; contacting a second sample containing the polypeptide with a second protease (e.g., Tryp-N); fragmenting the second set of digested peptide fragments to produce a second set of fragmented peptide ions; selecting pairs of peptide ions from the first and the second set of fragmented peptide ions that differ in mass by a mass of an arginine amino acid residue or a lysine amino acid residue; assigning an ion type (either N-terminal peptide ion or C-terminal peptide ion) to the selected pairs of the peptide ions from two sets of fragmented peptide ions; selecting a mass ladder of the same-type peptide ions in either set of fragmented peptide ions with incremental mass by the mass of amino acid residue(s), and assembling the identified amino acid residues from the mass ladder to determine the amino acid sequence of the polypeptide of interest.