Results 281 to 290 of about 483,403 (312)
Bioactive multi‐crosslinked hydrogels are prepared from gelatin methacrylate (GelMA), methacrylate‐functionalized alginate dialdehyde (ADAMA), and Cobalt‐doped mesoporous bioactive glass nanoparticles (Co‐MBGNs), demonstrating optimized elasticity, cytocompatibility, and wound healing potential.
Ehsan Zeimaran+4 more
wiley +1 more source
The abc's (and xyz's) of peptide sequencing [PDF]
Proteomics is an increasingly powerful and indispensable technology in molecular cell biology. It can be used to identify the components of small protein complexes and large organelles, to determine post-translational modifications and in sophisticated functional screens.
Matthias Mann, Hanno Steen
openaire +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Bioinformatics, 1986
A computer program has been devised to automate rationalization of peptide fragmentation patterns. The program systematically generates all possible linear amino acid sequences which might be attributable to a peptide with a known amino acid composition.
C. W. Hamm, W. E. Wilson, D. J. Harvan
openaire +3 more sources
A computer program has been devised to automate rationalization of peptide fragmentation patterns. The program systematically generates all possible linear amino acid sequences which might be attributable to a peptide with a known amino acid composition.
C. W. Hamm, W. E. Wilson, D. J. Harvan
openaire +3 more sources
Error-Tolerant Identification of Peptides in Sequence Databases by Peptide Sequence Tags
Analytical Chemistry, 1994We demonstrate a new approach to the identification of mass spectrometrically fragmented peptides. A fragmentation spectrum usually contains a short, easily identifiable series of sequence ions, which yields a partial sequence. This partial sequence divides the peptide into three parts-regions 1, 2, and 3-characterized by the added mass m1 of region 1,
Mann, M, Wilm, M
openaire +4 more sources
A method of peptide sequencing
Journal of the Chemical Society, Chemical Communications, 1973Sequencing of peptides has been carried out by degrading them to diketopiperazines and identification of the diketopiperazine by g.c./m.s. methods.
J. David Baty+2 more
openaire +3 more sources
Sequence‐assisted peptide synthesis (SAPS)
The Journal of Peptide Research, 1998Abstract:In solid‐phase peptide synthesis (SPPS) the growing peptide chain may undergo chain aggregation which can cause serious synthetic problems. A number of investigations concerning this problem have been reported in the chemical literature. During a study of such “difficult sequences” using the Fmoc‐protection strategy, we have observed that ...
Due Larsen, B., Holm, A.
openaire +3 more sources
Peptide sequencing by metastable mapping
Organic Mass Spectrometry, 1983AbstractThe amino acid sequence of three simple peptides has been determined by the technique of metastable mapping. The products of decompositions in the first field free region of a forward geometry double focussing mass spectrometer are studied by decreasing the electric sector field between scans of the magnetic field.
Urs Peter Schlunegger+3 more
openaire +2 more sources
The Dansyl-Edman Method for Peptide Sequencing [PDF]
The dansyl-Edman method for peptide sequencing uses the Edman degradation (see Chapter 26 ) to sequentially remove amino acids from the N-terminus of a peptide. Following the cleavage step of the Edman degradation, the thiazolinone derivative is extracted with an organic solvent and discarded.
openaire +3 more sources
Infrared spectroscopy of ‘forbidden’ peptide sequences [PDF]
Certain pentapeptide sequences are absent from all known universal protein primary structures, even though they are found in the non-coding regions of DNA. These 'forbidden' sequences may have been rejected by evolution because they disrupt the formation of functional secondary protein structures. The uncapped pentapeptides FFMCT and WCFNL, which model
Lavina C. Snoek+2 more
openaire +2 more sources
1991
For a recent American Society for Mass Spectrometry (ASMS) peptide sequencing workshop, some forty laboratories requested a sample of two unknown peptides. We chose to analyse a 1.5 μg sample with a stated mass of ~ 1800 u, and were the only laboratory to submit results on this peptide at the 1990 ASMS conference in Tucuon, Arizona.
Kenneth G. Standing+7 more
openaire +2 more sources
For a recent American Society for Mass Spectrometry (ASMS) peptide sequencing workshop, some forty laboratories requested a sample of two unknown peptides. We chose to analyse a 1.5 μg sample with a stated mass of ~ 1800 u, and were the only laboratory to submit results on this peptide at the 1990 ASMS conference in Tucuon, Arizona.
Kenneth G. Standing+7 more
openaire +2 more sources