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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    In biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its environment, such as by changing the temperature or pressure, pH, adding chemical denaturants, or applying force as with an atomic force microscope tip.

  4. Temperature gradient gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Temperature_gradient_gel...

    [1] [2] [3] The same equipment can be used for analysis of protein, which was first done by Thomas E. Creighton of the MRC Laboratory of Molecular Biology, Cambridge, England. [4] Similar looking patterns are produced by proteins and nucleic acids, but the fundamental principles are quite different.

  5. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  6. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Proteins, therefore, are usually denatured in the presence of a detergent such as sodium dodecyl sulfate (SDS) that coats the proteins with a negative charge. [3] Generally, the amount of SDS bound is relative to the size of the protein (usually 1.4g SDS per gram of protein), so that the resulting denatured proteins have an overall negative ...

  7. Gel electrophoresis of proteins - Wikipedia

    en.wikipedia.org/.../Gel_electrophoresis_of_proteins

    A very widespread discontinuous buffer system is the tris-glycine or "Laemmli" system that stacks at a pH of 6.8 and resolves at a pH of ~8.3-9.0. A drawback of this system is that these pH values may promote disulfide bond formation between cysteine residues in the proteins because the pKa of cysteine ranges from 8-9 and because reducing agent ...

  8. These 89 Appetizers Might Just Be The Best Part Of ... - AOL

    www.aol.com/89-appetizers-might-just-best...

    Pull-apart bread reaches a whole new level, thanks to brie and cranberry sauce. Use your favorite homemade sauce recipes, but store-bought works too if you're short for time.

  9. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    Outside the acceptable range of pH, proteins are denatured (i.e. their 3D structure is disrupted), causing enzymes and ion channels (among others) to malfunction. An acid–base imbalance is known as acidemia when the pH is acidic, or alkalemia when the pH is alkaline.