Institution
Applied Biosystems
About: Applied Biosystems is a based out in . It is known for research contribution in the topics: Mass spectrometry & Capillary electrophoresis. The organization has 1521 authors who have published 1579 publications receiving 285423 citations.
Topics: Mass spectrometry, Capillary electrophoresis, Nucleic acid, Oligonucleotide, Tandem mass spectrometry
Papers published on a yearly basis
Papers
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TL;DR: By using microbore HPLC methodology, a 14 kDa protein extremely homologous to Cystatin S, but amino-terminally extended by eight amino acids is discovered, becoming the first such protein to be discovered by this route.
17 citations
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TL;DR: Mass spectrometry and nuclear magnetic resonance analyses show that the ε-amino group of l-lysine is able to cross-link dihydroxylated aromatics, and potential applications in medicine or industry for biomaterials synthesised via the three component system consisting of the oligopeptide [Tyr-Lys]10, dihydrogenated aromatic and laccase are discussed.
Abstract: In order to design potential biomaterials, we investigated the laccase-catalyzed cross-linking between l-lysine or lysine-containing peptides and dihydroxylated aromatics. l-Lysine is one of the major components of naturally occurring mussel adhesive proteins (MAPs). Dihydroxylated aromatics are structurally related to 3,4-dihydroxyphenyl-l-alanine, another main component of MAPs. Mass spectrometry and nuclear magnetic resonance analyses show that the e-amino group of l-lysine is able to cross-link dihydroxylated aromatics. Additional oligomer and polymer cross-linked products were obtained from di- and oligopeptides containing l-lysine. Potential applications in medicine or industry for biomaterials synthesised via the three component system consisting of the oligopeptide [Tyr-Lys]10, dihydroxylated aromatics and laccase are discussed.
17 citations
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TL;DR: This investigation should provide further insight into synthesis options and cleavage protocols when working with cysteine-containing peptides.
Abstract: Fmoc-Cys(t-Bu)-OH, Fmoc-Cys(Acm)-OH, and Fmoc-Cys(Trt)-OH exhibit excellent synthesis characteristics when used in Fmoc solid phase peptide synthesis on the Applied Biosystems Model 431A peptide synthesizer. The actual 5% scavenger mixture will vary according to the particular amino acid residues present. As was previously mentioned, an anisole/ethanedithiol/ethylmethylsulfide mixture (3:1:1) works well as a general scavenger solution for TFA cleavage of Fmoc synthesized peptide resins. It also may be possible to use lower acid (TFA) concentrations. The syntheses and workups of the peptide Somatostatin utilizing these derivatives demonstrate the ease of using these cysteine derivatives with the Fmoc chemistry approach. The use of either the t-Bu or the Acm moiety produces a peptide containing protected thiol groups after cleavage with 95% TFA. The Fmoc-Cys(Trt)-OH derivative is efficiently deprotected using 95% TFA. This investigation should provide further insight into synthesis options and cleavage protocols when working with cysteine-containing peptides.
17 citations
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TL;DR: The utility of this technique with samples in the low picomole range is demonstrated to obtain useful sequence information following electrophoretic isolation of cyanogen bromide fragments purified by high performance electrophoresis chromatography.
17 citations
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TL;DR: The first proteomic analysis of the insoluble subproteome of the thermophilic bacterium Geobacillus thermoleovorans T80 is reported, and a number of proteins were identified that are known to be involved in the transport of compatible solutes,known to be important in microbial stress responses.
Abstract: To further our understanding of the biology of the thermophilic bacterium Geobacillus thermoleovorans T80, we now report the first proteomic analysis of the insoluble subproteome of this isolate. A combination of both shotgun and multidimensional methodologies were utilized, and a total of 8628 peptides was initially identified by automated MS/MS identification software. Curation of these peptides led to a final list of 184 positive protein identifications. The proteins from this insoluble subproteome were functionally classified, and physiochemical characterization was carried out. Of 15 hypothetical conserved proteins identified, we have assigned function to all but four. A total of 31 proteins were predicted to possess signal peptides. In silico investigation of these proteins allowed us to identify four of the five bacterial classes of signal peptide, namely, (i) twin-arginine translocation; (ii) Sec-type; (iii) lipoprotein, and (iv) ABC transport. In addition, a number of proteins were identified that are known to be involved in the transport of compatible solutes, known to be important in microbial stress responses.
17 citations
Authors
Showing all 1521 results
Name | H-index | Papers | Citations |
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Richard A. Gibbs | 172 | 889 | 249708 |
Friedrich C. Luft | 113 | 1095 | 47619 |
Alexander N. Glazer | 71 | 208 | 21068 |
Vineet Bafna | 68 | 236 | 42574 |
Kevin R. Coombes | 63 | 308 | 23592 |
Darryl J. Pappin | 61 | 170 | 29409 |
Mark D. Johnson | 60 | 289 | 16103 |
György Marko-Varga | 56 | 409 | 12600 |
Paul Thomas | 56 | 128 | 44810 |
Gerald Zon | 55 | 256 | 11126 |
Michael W. Hunkapiller | 51 | 130 | 29756 |
Bjarni V. Halldorsson | 51 | 145 | 13180 |
David H. Hawke | 50 | 157 | 9824 |
Ellson Y. Chen | 50 | 71 | 28836 |
Sridhar Hannenhalli | 49 | 162 | 21959 |