| pubmed-article:11838016 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11838016 | lifeskim:mentions | umls-concept:C0028263 | lld:lifeskim |
| pubmed-article:11838016 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:11838016 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
| pubmed-article:11838016 | lifeskim:mentions | umls-concept:C0282597 | lld:lifeskim |
| pubmed-article:11838016 | lifeskim:mentions | umls-concept:C0349590 | lld:lifeskim |
| pubmed-article:11838016 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11838016 | pubmed:dateCreated | 2002-2-11 | lld:pubmed |
| pubmed-article:11838016 | pubmed:abstractText | The so-called "chemical noise background" imposes a major limit on the practical sensitivity of MALDI mass spectrometry. Typically, as the amount of material of interest subjected to MALDI analysis is reduced, the signal decreases to the point where it can no longer be differentiated from the chemical noise. Using a newly designed MALDI-ion trap mass spectrometer, we describe experiments intended to throw light on the nature of the chemical noise background and to reduce its effects. Single-stage mass spectrometric signals from peptides were observed to disappear into the noise when the amount of sample applied to the MALDI sample stage was decreased to less than a femtomole. At these low levels, analysis of the collision-induced fragmentation spectra revealed the presence of ions originating from the peptide as well as cluster ions that originate from the chemical noise. The fragmentation pattern arising from dissociation of the cluster species suggests that they are composed largely of matrix molecules. A significant fraction of these cluster ions can be dissociated at activation energies lower than the threshold for peptide fragmentation. We used this finding to collisionally pre-activate MALDI ions to remove a significant portion of the chemical noise from the spectrum, allowing us to obtain readily discernible single stage MS signals from 100 attomols of peptide. The strategy also yielded high quality MS/MS spectra from 100 attomols of peptide. Different possibilities of collisional pre-activation for improving sensitivity are considered. | lld:pubmed |
| pubmed-article:11838016 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11838016 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11838016 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:11838016 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11838016 | pubmed:issn | 1044-0305 | lld:pubmed |
| pubmed-article:11838016 | pubmed:author | pubmed-author:ChaitBrian... | lld:pubmed |
| pubmed-article:11838016 | pubmed:author | pubmed-author:KrutchinskyAn... | lld:pubmed |
| pubmed-article:11838016 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11838016 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:11838016 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11838016 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11838016 | pubmed:pagination | 129-34 | lld:pubmed |
| pubmed-article:11838016 | pubmed:dateRevised | 2003-11-3 | lld:pubmed |
| pubmed-article:11838016 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11838016 | pubmed:articleTitle | On the nature of the chemical noise in MALDI mass spectra. | lld:pubmed |
| pubmed-article:11838016 | pubmed:affiliation | Rockefeller University, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:11838016 | pubmed:publicationType | Journal Article | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11838016 | lld:pubmed |
