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IPC – Isoelectric Point Calculator — calculate protein isoelectric point using over 15 methods prot pi – protein isoelectric point — an online program for calculating pI of proteins (include multiple subunits and posttranslational modifications)
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 ...
It was first defined by S.P.L. Sørensen, Kaj Ulrik Linderstrøm-Lang and Ellen Lund in 1926 [1] and is mainly a term used in protein sciences. It is different from the isoelectric point (pI) in that pI is the pH value at which the net charge of the molecule, including bound ions is zero. Whereas the isoionic point is at net charge zero in a ...
Calculate how much protein you need according to your body weight. Molloy advises people to eat about 0.75 grams of protein per pound of total body mass, or 1.6 grams per kilogram.
Protein–protein interaction prediction is a field combining bioinformatics and structural biology in an attempt to identify and catalog physical interactions between pairs or groups of proteins. Understanding protein–protein interactions is important for the investigation of intracellular signaling pathways, modelling of protein complex ...
The isoelectric point (pI) is the pH of a solution at which the net primary charge of a protein becomes zero. At a solution pH that is above the pI the surface of the protein is predominantly negatively charged and therefore like-charged molecules will exhibit repulsive forces.
Protein structure is a complex mosaic of various dielectric medium generated by arrangement of different amino acids. Hence, different parts of the protein structure most likely would behave as solvents with different dielectric values.
Analyzing the shape of the plot gives information about partial structure of the protein. For instance, if a stretch of about 20 amino acids shows positive for hydrophobicity, these amino acids may be part of alpha-helix spanning across a lipid bilayer, which is composed of hydrophobic fatty acids. On the converse, amino acids with high ...