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  2. Dialysis (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Dialysis_(chemistry)

    Dialysis is the process used to change the matrix of molecules in a sample by differentiating molecules by the classification of size. [6] [7] It relies on diffusion, which is the random, thermal movement of molecules in solution (Brownian motion) that leads to the net movement of molecules from an area of higher concentration to a lower concentration until equilibrium is reached.

  3. Desalting and buffer exchange - Wikipedia

    en.wikipedia.org/wiki/Desalting_and_buffer_exchange

    Desalting and buffer exchange both entail recovering the components of a sample in whatever buffer is used to pre-equilibrate the small, porous polymer beads (resin). Desalting occurs when buffer salts and other small molecules are removed from a sample in exchange for water (with the resin being pre-equilibrated in water).

  4. Fast protein liquid chromatography - Wikipedia

    en.wikipedia.org/wiki/Fast_protein_liquid...

    Fast protein liquid chromatography (FPLC) is a form of liquid chromatography that is often used to analyze or purify mixtures of proteins. As in other forms of chromatography, separation is possible because the different components of a mixture have different affinities for two materials, a moving fluid (the mobile phase) and a porous solid (the stationary phase).

  5. Phosphate-buffered saline - Wikipedia

    en.wikipedia.org/wiki/Phosphate-buffered_saline

    There are many different ways to prepare PBS solutions, common ones are Dulbecco's phosphate-buffered saline (DPBS) [2] and the Cold Spring Harbor protocol. [3] Some formulations of DPBS do not contain potassium and magnesium, while other ones contain calcium and/or magnesium (depending on whether or not the buffer is used on live or fixed tissue: the latter does not require CaCl 2 or MgCl 2).

  6. Diafiltration - Wikipedia

    en.wikipedia.org/wiki/Diafiltration

    Diafiltration for Desalting or Buffer Exchange; Mobius Ultra/ Diafiltration Solutions This page was last ...

  7. Protein purification - Wikipedia

    en.wikipedia.org/wiki/Protein_purification

    Anion exchange resins have a positive charge and are used to retain and separate negatively charged compounds (anions), while cation exchange resins have a negative charge and are used to separate positively charged molecules (cations). Before the separation begins a buffer is pumped through the column to equilibrate the opposing charged ions.

  8. Size-exclusion chromatography - Wikipedia

    en.wikipedia.org/wiki/Size-exclusion_chromatography

    Ion exchange chromatography Micellar liquid chromatography Size-exclusion chromatography , also known as molecular sieve chromatography , [ 1 ] is a chromatographic method in which molecules in solution are separated by their shape , and in some cases size . [ 2 ]

  9. Isothermal titration calorimetry - Wikipedia

    en.wikipedia.org/wiki/Isothermal_Titration...

    The compounds to be studied are placed in the sample cell, while the other cell, the reference cell, is used as a control and contains the buffer in which the sample is dissolved. The technique was developed by H. D. Johnston in 1968 as a part of his Ph.D. dissertation at Brigham Young University, [ 5 ] and was considered niche until introduced ...