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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. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates.

  4. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structure is the three-dimensional arrangement of atoms in an amino acid -chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer.

  5. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    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. [1][2] If the equilibrium was maintained at all ...

  6. Protein aggregation - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation

    Misfolded proteins can form protein aggregates or amyloid fibrils, get degraded, or refold back to its native structure. In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. [ 1 ][ 2 ] Protein ...

  7. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Overview of gel electrophoresis. Electrophoresis is a process that enables the sorting of molecules based on charge, size, or shape. Using an electric field, molecules (such as DNA) can be made to move through a gel made of agarose or polyacrylamide. The electric field consists of a negative charge at one end which pushes the molecules through ...

  8. 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.

  9. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Proteolysis in organisms serves many purposes; for ...