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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 the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.

  4. Globular protein - Wikipedia

    en.wikipedia.org/wiki/Globular_protein

    Even in the protein's denatured state, it can be folded into the correct structure. Globular proteins seem to have two mechanisms for protein folding, either the diffusion-collision model or nucleation condensation model, although recent findings have shown globular proteins, such as PTP-BL PDZ2, that fold with characteristic features of both ...

  5. Chemoproteomics - Wikipedia

    en.wikipedia.org/wiki/Chemoproteomics

    Additionally, many identified enzymes have not been sufficiently characterized to yield actionable mechanisms on which to base functional assays. Without a basis for a functional biochemical readout , chemical tools are required to detect drug-protein interactions.

  6. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes are not rigid, static structures; instead they have complex internal dynamic motions – that is, movements of parts of the enzyme's structure such as individual amino acid residues, groups of residues forming a protein loop or unit of secondary structure, or even an entire protein domain.

  7. Proteinase K - Wikipedia

    en.wikipedia.org/wiki/Proteinase_K

    It is highly suited to this application since the enzyme is active in the presence of chemicals that denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is used for the destruction of proteins in cell lysates (tissue, cell culture cells) and for ...

  8. Experts Say This Is What Actually Happens When You Dissolve ...

    www.aol.com/experts-actually-happens-dissolve...

    Whether you're getting a haircut, altering your brow shape, or getting lip filler, deciding to change your appearance is a pretty big commitment.And the thought of being faced with results you don ...

  9. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...