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FDPB-based methods calculate the change in the pK a value of an amino acid side chain when that side chain is moved from a hypothetical fully solvated state to its position in the protein. To perform such a calculation, one needs theoretical methods that can calculate the effect of the protein interior on a p K a value, and knowledge of the pKa ...
In this updated version it is possible to determine insulin sensitivity and β-cell function from paired fasting plasma glucose and radioimmunoassay insulin, specific insulin, or C-peptide concentrations. The authors recommend the computer software be used wherever possible.
The Wimley–White whole residue hydrophobicity scales are significant for two reasons. First, they include the contributions of the peptide bonds as well as the sidechains, providing absolute values. Second, they are based on direct, experimentally determined values for transfer free energies of polypeptides.
Unlike relative quantification, though, the abundance of the target peptide in the experimental sample is compared to that of the heavy peptide and back-calculated to the initial concentration of the standard using a pre-determined standard curve to yield the absolute quantification of the target peptide.
At the peptide level, the signals of the reporter ions of each MS/MS spectrum allow for calculating the relative abundance (ratio) of the peptide(s) identified by this spectrum. [ citation needed ] The abundance of the reporter ions may consist of more than one single signal in the MS/MS data and the signals have to be integrated in some way ...
TDEE is the number of calories you need to maintain your current weight based on your activity level. From there, you can adjust your calorie intake to create a deficit for weight loss. For ...
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).
Label-free quantification experiment with 3 samples, 3 LC-MS files and 5 precursor ions/peptides. Intensities at the peak of the chromatographic peaks are used for quantification in this particular case. Peptides are identified via fragmentation mass spectra, and some of the precursor ions will be quantified, but not mapped to any peptide sequence.