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  2. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    Amino acids that make up proteins may be positive, negative, neutral, or polar in nature, and together give a protein its overall charge. At a pH below their pI, proteins carry a net positive charge; above their pI they carry a net negative charge. Proteins can, thus, be separated by net charge in a polyacrylamide gel using either preparative ...

  3. Electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Electrophoresis

    The technique normally applies a negative charge called cathode so anionic protein molecules move towards a positive charge called anode. [2] Therefore, electrophoresis of positively charged particles or molecules ( cations ) is sometimes called cataphoresis , while electrophoresis of negatively charged particles or molecules (anions) is ...

  4. Symporter - Wikipedia

    en.wikipedia.org/wiki/Symporter

    Second, large groups of predominantly positively charged or negatively charged particles will naturally repel each other. This is demonstrated by attempting to push the two positive poles or two negative poles of a magnet together.

  5. Membrane potential - Wikipedia

    en.wikipedia.org/wiki/Membrane_potential

    The membrane potential in a cell derives ultimately from two factors: electrical force and diffusion. Electrical force arises from the mutual attraction between particles with opposite electrical charges (positive and negative) and the mutual repulsion between particles with the same type of charge (both positive or both negative).

  6. Protein adsorption - Wikipedia

    en.wikipedia.org/wiki/Protein_adsorption

    There are several types of common lattice formations, and each has its own unique packing density and atomic closeness. The negatively charged electron clouds of the metal ions will sterically hinder the adhesion of negatively charged protein regions due to charge repulsion, thus limiting the available binding sites of a protein to a metal surface.

  7. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    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. Likewise, at a solution pH that is below the pI, the surface of the protein is predominantly positively charged and repulsion between proteins occurs.

  8. Ion chromatography - Wikipedia

    en.wikipedia.org/wiki/Ion_chromatography

    The amino acids that have negatively charged side chains at pH 7 (pH of water) are glutamate and aspartate. The beads that are negatively charged are called cation exchange resins, as positively charged proteins will be attracted. The amino acids that have positively charged side chains at pH 7 are lysine, histidine and arginine. [48]

  9. Gibbs–Donnan effect - Wikipedia

    en.wikipedia.org/wiki/Gibbs–Donnan_effect

    In many instances, from ultrafiltration of proteins to ion exchange chromatography, the pH of the buffer adjacent to the charged groups of the membrane is different from the pH of the rest of the buffer solution. [6] When the charged groups are negative (basic), then they will attract protons so that the pH will be lower than the surrounding ...