Abstract: A method of mass spectrometry is disclosed comprising mass analysing an eluent from a chromatography device and obtaining parent ion data sets and corresponding product ion data sets, and determining whether, in a first product ion data set, one or more product ions are present that are related to one or more parent ions in a corresponding first parent ion data set, based on the mass or mass to charge ratio and/or intensity of the one or more product ions and the one or more parent ions. If it is determined that the one or more product ions are present, the method further comprises removing the one or more product ions from one or more second product ion data sets to produce one or more second modified product ion data sets and/or removing ions other than the one or more product ions from the first product ion data set to produce a first modified product ion data set.

Abstract: The present disclosure generally relates to methods for determining chemical class compositions present in a sample using collision cross-section fragment ion values.

Abstract: The present disclosure generally relates to methods for determining chemical class compositions present in a sample using collision cross-section fragment ion values.

Abstract: A method of mass spectrometry is disclosed comprising mass analysing an eluent from a chromatography device and obtaining parent ion data sets and corresponding product ion data sets, and determining whether, in a first product ion data set, one or more product ions are present that are related to one or more parent ions in a corresponding first parent ion data set, based on the mass or mass to charge ratio and/or intensity of the one or more product ions and the one or more parent ions. If it is determined that the one or more product ions are present, the method further comprises removing the one or more product ions from one or more second product ion data sets to produce one or more second modified product ion data sets and/or removing ions other than the one or more product ions from the first product ion data set to produce a first modified product ion data set.

Abstract: Absolute quantitation of protein in a sample is provided by comparing a sum or average of the N highest ionization intensities observed for peptides of a particular protein along with a calibration standard. The calibration standard can be in the form of a table generated by prior protein peptide analysis performed using one or more pre-determined proteins. The comparison is used to determine a corresponding absolute quantity of protein based on the observed sum or average of ionization intensities. A simple conversion factor can be applied to the calibration standard value to determine the absolute quantity of protein in the sample.

Abstract: Techniques are described for matching a precursor ion with one or more related product ions. Input data sets are obtained from a plurality of injections. Each of the input data sets includes a same precursor ion and one or more product ions. The input data sets are normalized in accordance with a single retention time for the precursor ion. For each input data set, it is determined which product ions are within a predetermined retention time window with respect to the single retention time for the precursor ion. If a product ion is within the predetermined retention time window in at least one of the input data sets, it is determined that the product ion is related to the precursor ion. An apparatus for analyzing a sample includes a chromatography module, a mass-spectrometry module, and a control unit.

Abstract: Absolute quantitation of protein in a sample is provided by comparing a sum or average of the N highest ionization intensities observed for peptides of a particular protein along with a calibration standard. The calibration standard can be in the form of a table generated by prior protein peptide analysis performed using one or more pre-determined proteins. The comparison is used to determine a corresponding absolute quantity of protein based on the observed sum or average of ionization intensities. A simple conversion factor can be applied to the calibration standard value to determine the absolute quantity of protein in the sample.

Abstract: A method for matching a precursor ion with one or more related product ions includes providing input data sets obtained from sample injections, each of the data sets including a precursor ion and one or more product ions, normalizing the input data sets in accordance with a single retention time for the precursor ion, determining which product ions are within a predetermined retention time window with respect to the single retention time, and, if a product ion is within the predetermined retention time window for a specified number of the input data sets, determining that the product ion is related to the precursor having the single retention time. An apparatus for analyzing a sample includes a chromatography module, a mass-spectrometry module in communication with the chromatography module, and control unit in communication with the chromatography module and the mass-spectrometry module.

Abstract: Absolute quantitation of protein in a sample is provided by comparing a sum or average of the N highest ionization intensities observed for peptides of a particular protein along with a calibration standard. The calibration standard can be in the form of a table generated by prior protein peptide analysis performed using one or more pre-determined proteins. The comparison is used to determine a corresponding absolute quantity of protein based on the observed sum or average of ionization intensities. A simple conversion factor can be applied to the calibration standard value to determine the absolute quantity of protein in the sample.

Abstract: A method (100) for performing chemical analyses includes digesting a reference sample to obtain precursors associated with a peptide in the sample (110), separating the precursors to determine values associated with retention times of the separated precursors (120), ionizing the separated precursors to form precursor ions (130), mass analyzing the precursor ions to determine values associated with mass and with ion intensity (140), and storing a <fcfile of the polypeptide defined by the determined values (150). A subject sample is analyzed (160), and the polypeptide is detected in the subject sample in response to a match between subject-sample and profile values. An apparatus (900) for performing chemical analyses includes a chromatography module (904), a mass-spectrometry module (912), and a computer module (926).

Abstract: A method of identifying molecules of biological origin is disclosed. The molecules are identified and the basis of the accurately determined mass to charge ratio of the molecules and at least a further physico-chemical property such as elution time or charge state. Further physico-chemical properties may be used. The experimentally determined accurate mass and physico-chemical properties can then be compared with a look-up table of information. The look-up table may generated or physico-chemical properties of data in a conventional database may be calculated. The ability to recognize and preferably identify the same molecules in two different samples may be used to determine whether a particular biological molecules has been expressed differently in an experimental sample relative to a control sample.

Abstract: Techniques are described for matching a precursor ion with one or more related product ions, including providing a plurality of input data sets obtained from a plurality of injections, each of the plurality of input data sets including a same precursor ion and one or more product ions, normalizing the plurality of input data sets in accordance with a single retention time for the precursor ion, for each of the plurality of input data sets, determining which product ions are within a predetermined retention time window with respect to the single retention time for the precursor ion, and if a product ion is within the predetermined retention time window in at least one of the plurality of input data sets, determining that the product ion is related to the precursor ion having the single retention time

Abstract: Absolute quantitation of protein in a sample is provided by comparing a sum or average of the N highest ionization intensities observed for peptides of a particular protein along with a calibration standard. The calibration standard can be in the form of a table generated by prior protein peptide analysis performed using one or more pre-determined proteins. The comparison is used to determine a corresponding absolute quantity of protein based on the observed sum or average of ionization intensities. A simple conversion factor can be applied to the calibration standard value to determine the absolute quantity of protein in the sample.

Abstract: A method of identifying molecules of biological origin is disclosed. The molecules are identified and the basis of the accurately determined mass to charge ratio of the molecules and at least a further physico-chemical property such as elution time or charge state. Further physico-chemical properties may be used. The experimentally determined accurate mass and physico-chemical properties can then be compared with a look-up table of information. The look-up table may generated or physico-chemical properties of data in a conventional database may be calculated. The ability to recognise and preferably identify the same molecules in two different samples may be used to determine whether a particular biological molecules has been expressed differently in an experimental sample relative to a control sample.

Abstract: A method of identifying molecules of biological origin is disclosed. The molecules are identified and the basis of the accurately determined mass to charge ratio of the molecules and at least a further physico-chemical property such as elution time or charge state. Further physico-chemical properties may be used. The experimentally determined accurate mass and physico-chemical properties can then be compared with a look-up table of information. The look-up table may generated or physico-chemical properties of data in a conventional database may be calculated. The ability to recognise and preferably identify the same molecules in two different samples may be used to determine whether a particular biological molecules has been expressed differently in an experimental sample relative to a control sample.

Abstract: A method of identifying molecules of biological origin is disclosed. The molecules are identified and the basis of the accurately determined mass to charge ratio of the molecules and at least a further physico-chemical property such as elution time or charge state. Further physico-chemical properties may be used. The experimentally determined accurate mass and physico-chemical properties can then be compared with a look-up table of information. The look-up table may generated or physico-chemical properties of data in a conventional database may be calculated. The ability to recognise and preferably identify the same molecules in two different samples may be used to determine whether a particular biological molecules has been expressed differently in an experimental sample relative to a control sample.

Abstract: A system and method for mass analysis where a sample (102) is separated in a liquid chromatograph (104), and subsequently analyzed in a mass spectrometer (112).

Abstract: A method of identifying molecules of biological origin is disclosed. The molecules are identified and the basis of the accurately determined mass to charge ratio of the molecules and at least a further physico-chemical property such as elution time or charge state. Further physico-chemical properties may be used. The experimentally determined accurate mass and physico-chemical properties can then be compared with a look-up table of information. The look-up table may generated or physico-chemical properties of data in a conventional database may be calculated. The ability to recognise and preferably identify the same molecules in two different samples may be used to determine whether a particular biological molecules has been expressed differently in an experimental sample relative to a control sample.

Abstract: A method of identifying molecules of biological origin is disclosed. The molecules are identified and the basis of the accurately determined mass to charge ratio of the molecules and at least a further physico-chemical property such as elution time or charge state. Further physico-chemical properties may be used. The experimentally determined accurate mass and physico-chemical properties can then be compared with a look-up table of information. The look-up table may generated or physico-chemical properties of data in a conventional database may be calculated. The ability to recognise and preferably identify the same molecules in two different samples may be used to determine whether a particular biological molecules has been expressed differently in an experimental sample relative to a control sample.