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  2. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein folding must be thermodynamically favorable within a cell in order for it to be a spontaneous reaction. Since it is known that protein folding is a spontaneous reaction, then it must assume a negative Gibbs free energy value. Gibbs free energy in protein folding is directly related to enthalpy and entropy. [12]

  3. Osteoclast - Wikipedia

    en.wikipedia.org/wiki/Osteoclast

    At a site of active bone resorption, the osteoclast forms a specialized cell membrane, the "ruffled border", that opposes the surface of the bone tissue. This extensively folded or ruffled border facilitates bone removal by dramatically increasing the cell surface for secretion and uptake of the resorption compartment contents and is a ...

  4. Fibrocyte - Wikipedia

    en.wikipedia.org/wiki/Fibrocyte

    Fibroblasts are activated connective tissue cells characterized by synthesis of proteins of the fibrous matrix, particularly the collagens. When tissue is injured, the predominant mesenchymal cells, the fibroblast, have been believed to be derived from the fibrocyte or possibly from smooth muscle cells lining vessels and glands.

  5. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    Folding is a directed search of conformational space allowing the protein to fold on a biologically feasible time scale. The Levinthal paradox states that if an averaged sized protein would sample all possible conformations before finding the one with the lowest energy, the whole process would take billions of years. [ 52 ]

  6. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    A protein folded into its native state or native conformation typically has a lower Gibbs free energy (a combination of enthalpy and entropy) than the unfolded conformation.A protein will tend towards low-energy conformations, which will determine the protein's fold in the cellular environment.

  7. Protein fold class - Wikipedia

    en.wikipedia.org/wiki/Protein_fold_class

    Numerous protein structures are the result of rational design and do not exist in nature. Proteins can be designed from scratch (de novo design) or by making calculated variations on a known protein structure and its sequence (known as protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to ...

  8. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation.

  9. Chondrocyte - Wikipedia

    en.wikipedia.org/wiki/Chondrocyte

    Endochondral ossification is the process by which most vertebrate axial skeletons form into hardened bones from cartilage. This process begins with a cartilage anlage where chondrocyte cells will congregate and start their maturation process. Once the chondrocytes have fully matured at the desired rate, the cartilage tissue will harden into ...