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The mass of b 2-ion = mass of two amino acid residues + 1. Table 2. Mass of b2-ions in peptide fragmentation [16] Identify a sequence ion series by the same mass difference, which matches one of the amino acid residue masses (see Table 1). For example, mass differences between a n and a n-1, b n and b n-1, c n and c n-1 are the same.
The monoisotopic mass is very useful when analyzing small organic compounds since compounds with similar weights will not be differentiated if the nominal mass is used. For example, when comparing tyrosine which has a molecular structure of C 9 H 11 NO 3 with a monoisotopic mass of 182.081 Da and methionine sulphone C 5 H 11 NO 4 S which ...
Palmitic acid (hexadecanoic acid in IUPAC nomenclature) is a fatty acid with a 16-carbon chain. It is the most common saturated fatty acid found in animals, plants and microorganisms. [ 9 ] [ 10 ] Its chemical formula is CH 3 (CH 2 ) 14 COOH , and its C:D ratio (the total number of carbon atoms to the number of carbon-carbon double bonds) is 16:0.
Palmitoyl-CoA is an acyl-CoA thioester. It is an "activated" form of palmitic acid and can be transported into the mitochondrial matrix by the carnitine shuttle system (which transports fatty acyl-CoA molecules into the mitochondria), and once inside can participate in beta-oxidation.
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The monoisotopic substrate and a deuterated form of the substrate are separately exposed to the enzyme of interest over a range of concentrations. The Michaelis-Menten kinetic parameters for both substrates are determined and the position-specific isotope effect at the site of deuteration is expressed as the ratio of the monoisotopic rate ...
The monoisotopic mass is the sum of the masses of the atoms in a molecule using the unbound, ground-state, rest mass of the principal (most abundant) isotope for each element. [12] [5] The monoisotopic mass of a molecule or ion is the exact mass obtained using the principal isotopes. Monoisotopic mass is typically expressed in daltons.
A typical workflow of a peptide mass fingerprinting experiment. Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. [1]