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  2. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    Proteinprotein interactions regulate enzymatic activity, control progression through the cell cycle, and allow the assembly of large protein complexes that carry out many closely related reactions with a common biological function. Proteins can bind to, or be integrated into, cell membranes.

  3. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structure databases are critical for many efforts in computational biology such as structure based drug design, both in developing the computational methods used and in providing a large experimental dataset used by some methods to provide insights about the function of a protein.

  4. 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]

  5. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    There is a commonality of stable tertiary structures seen in proteins of diverse function and diverse evolution. For example, the TIM barrel, named for the enzyme triosephosphateisomerase, is a common tertiary structure as is the highly stable, dimeric, coiled coil structure. Hence, proteins may be classified by the structures they hold.

  6. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Proteins are often synthesized in an inactive precursor form; typically, an N-terminal or C-terminal segment blocks the active site of the protein, inhibiting its function. The protein is activated by cleaving off the inhibitory peptide. Some proteins even have the power to cleave themselves.

  7. Central dogma of molecular biology - Wikipedia

    en.wikipedia.org/wiki/Central_dogma_of_molecular...

    For most proteins it requires other chaperone proteins to control the form of the product. Some proteins then excise internal segments from their own peptide chains, splicing the free ends that border the gap; in such processes the inside "discarded" sections are called inteins. Other proteins must be split into multiple sections without splicing.

  8. Eating More Protein to Lose Weight? Avoid These 6 Common Mistakes

    www.aol.com/eating-more-protein-lose-weight...

    Protein is a vital part of a well-balanced diet, assisting with organ function and muscle growth and maintenance. ... which make up the protein,” Cohn said. “Every single amino acid works ...

  9. Protein quaternary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_quaternary_structure

    Protein quaternary structure [a] is the fourth (and highest) classification level of protein structure.Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits).