The Experts below are selected from a list of 25824 Experts worldwide ranked by ideXlab platform
Knut Reinert - One of the best experts on this subject based on the ideXlab platform.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses. Results We have introduced two novel MS calibration methods. The first method utilises the local similarity of peptide maps generated after separation of complex protein samples by two-dimensional gel electrophoresis. It computes a multiple peak-list alignment of the Data set using a modified Minimum Spanning Tree (MST) algorithm. The second method exploits the idea that hundreds of MS samples are measured in parallel on one sample support. It improves the calibration coefficients by applying a two-dimensional Thin Plate Splines (TPS) smoothing algorithm. We studied the novel calibration methods utilising Data generated by three different MALDI-TOF-MS instruments. We demonstrate that a PMF Data set can be calibrated without resorting to external or relying on widely occurring internal calibrants. The methods developed here were implemented in R and are part of the BioConductor package mscalib available from http://www.bioconductor.org . Conclusion The MST calibration algorithm is well suited to calibrate MS spectra of protein samples resulting from two-dimensional gel electrophoretic separation. The TPS based calibration algorithm might be used to correct systematic mass measurement errors observed for large MS sample supports. As compared to other methods, our combined MS spectra calibration strategy increases the peptide/protein identification rate by an additional 5 – 15%.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses.
Witold E Wolski - One of the best experts on this subject based on the ideXlab platform.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses. Results We have introduced two novel MS calibration methods. The first method utilises the local similarity of peptide maps generated after separation of complex protein samples by two-dimensional gel electrophoresis. It computes a multiple peak-list alignment of the Data set using a modified Minimum Spanning Tree (MST) algorithm. The second method exploits the idea that hundreds of MS samples are measured in parallel on one sample support. It improves the calibration coefficients by applying a two-dimensional Thin Plate Splines (TPS) smoothing algorithm. We studied the novel calibration methods utilising Data generated by three different MALDI-TOF-MS instruments. We demonstrate that a PMF Data set can be calibrated without resorting to external or relying on widely occurring internal calibrants. The methods developed here were implemented in R and are part of the BioConductor package mscalib available from http://www.bioconductor.org . Conclusion The MST calibration algorithm is well suited to calibrate MS spectra of protein samples resulting from two-dimensional gel electrophoretic separation. The TPS based calibration algorithm might be used to correct systematic mass measurement errors observed for large MS sample supports. As compared to other methods, our combined MS spectra calibration strategy increases the peptide/protein identification rate by an additional 5 – 15%.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses.
Raimond N J Veldhuis - One of the best experts on this subject based on the ideXlab platform.
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practical biometric authentication with template protection
Lecture Notes in Computer Science, 2005Co-Authors: Pim Theo Tuyls, Anton H M Akkermans, Tom A M Kevenaar, Geertjan Schrijen, A M Bazen, Raimond N J VeldhuisAbstract:In this paper we show the feasibility of template protecting biometric authentication systems. In particular, we apply template protection schemes to Fingerprint Data. Therefore we first make a fixed length representation of the Fingerprint Data by applying Gabor filtering. Next we introduce the reliable components scheme. In order to make a binary representation of the Fingerprint images we extract and then quantize during the enrollment phase the reliable components with the highest signal to noise ratio. Finally, error correction coding is applied to the binary representation. It is shown that the scheme achieves an EER of approximately 4.2% with secret length of 40 bits in experiments.
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AVBPA - Practical biometric authentication with template protection
Lecture Notes in Computer Science, 2005Co-Authors: Pim Theo Tuyls, Anton H M Akkermans, Tom A M Kevenaar, Geertjan Schrijen, A M Bazen, Raimond N J VeldhuisAbstract:In this paper we show the feasibility of template protecting biometric authentication systems. In particular, we apply template protection schemes to Fingerprint Data. Therefore we first make a fixed length representation of the Fingerprint Data by applying Gabor filtering. Next we introduce the reliable components scheme. In order to make a binary representation of the Fingerprint images we extract and then quantize during the enrollment phase the reliable components with the highest signal to noise ratio. Finally, error correction coding is applied to the binary representation. It is shown that the scheme achieves an EER of approximately 4.2% with secret length of 40 bits in experiments.
Peter Jungblut - One of the best experts on this subject based on the ideXlab platform.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses. Results We have introduced two novel MS calibration methods. The first method utilises the local similarity of peptide maps generated after separation of complex protein samples by two-dimensional gel electrophoresis. It computes a multiple peak-list alignment of the Data set using a modified Minimum Spanning Tree (MST) algorithm. The second method exploits the idea that hundreds of MS samples are measured in parallel on one sample support. It improves the calibration coefficients by applying a two-dimensional Thin Plate Splines (TPS) smoothing algorithm. We studied the novel calibration methods utilising Data generated by three different MALDI-TOF-MS instruments. We demonstrate that a PMF Data set can be calibrated without resorting to external or relying on widely occurring internal calibrants. The methods developed here were implemented in R and are part of the BioConductor package mscalib available from http://www.bioconductor.org . Conclusion The MST calibration algorithm is well suited to calibrate MS spectra of protein samples resulting from two-dimensional gel electrophoretic separation. The TPS based calibration algorithm might be used to correct systematic mass measurement errors observed for large MS sample supports. As compared to other methods, our combined MS spectra calibration strategy increases the peptide/protein identification rate by an additional 5 – 15%.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses.
Maciej Lalowski - One of the best experts on this subject based on the ideXlab platform.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses. Results We have introduced two novel MS calibration methods. The first method utilises the local similarity of peptide maps generated after separation of complex protein samples by two-dimensional gel electrophoresis. It computes a multiple peak-list alignment of the Data set using a modified Minimum Spanning Tree (MST) algorithm. The second method exploits the idea that hundreds of MS samples are measured in parallel on one sample support. It improves the calibration coefficients by applying a two-dimensional Thin Plate Splines (TPS) smoothing algorithm. We studied the novel calibration methods utilising Data generated by three different MALDI-TOF-MS instruments. We demonstrate that a PMF Data set can be calibrated without resorting to external or relying on widely occurring internal calibrants. The methods developed here were implemented in R and are part of the BioConductor package mscalib available from http://www.bioconductor.org . Conclusion The MST calibration algorithm is well suited to calibrate MS spectra of protein samples resulting from two-dimensional gel electrophoretic separation. The TPS based calibration algorithm might be used to correct systematic mass measurement errors observed for large MS sample supports. As compared to other methods, our combined MS spectra calibration strategy increases the peptide/protein identification rate by an additional 5 – 15%.
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Calibration of mass spectrometric peptide mass Fingerprint Data without specific external or internal calibrants
BMC Bioinformatics, 2005Co-Authors: Witold E Wolski, Maciej Lalowski, Peter Jungblut, Knut ReinertAbstract:Background Peptide Mass Fingerprinting (PMF) is a widely used mass spectrometry (MS) method of analysis of proteins and peptides. It relies on the comparison between experimentally determined and theoretical mass spectra. The PMF process requires calibration, usually performed with external or internal calibrants of known molecular masses.