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  2. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    Because many similar conformations will have similar energies, protein structures are dynamic, fluctuating between these similar structures. Globular proteins have a core of hydrophobic amino acid residues and a surface region of water-exposed, charged, hydrophilic residues. This arrangement may stabilize interactions within the tertiary structure.

  3. 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

  4. Tetrameric protein - Wikipedia

    en.wikipedia.org/wiki/Tetrameric_protein

    Hydrogen bonding networks between subunits has been shown to be important for the stability of the tetrameric quaternary protein structure.For example, a study of SDH which used diverse methods such as protein sequence alignments, structural comparisons, energy calculations, gel filtration experiments and enzyme kinetics experiments, could reveal an important hydrogen bonding network which ...

  5. 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 ...

  6. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    Pyruvate kinase, a protein with three domains (In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of ...

  7. Bivalent (genetics) - Wikipedia

    en.wikipedia.org/wiki/Bivalent_(genetics)

    The structure, visible by microscopy, is called a bivalent. [5] Resolution of the DNA recombination intermediate into a crossover exchanges DNA segments between the two homologous chromosomes at a site called a chiasma (plural: chiasmata). This physical strand exchange and the cohesion between the sister chromatids along each chromosome ensure ...

  8. Forget crunches: The smarter way to strengthen your core - AOL

    www.aol.com/news/core-why-does-matter-140042494.html

    Whether you want better balance, more powerful movements, or fewer backaches and injuries in the new year or any time of year, your core holds the key. Read on to learn why core health matters and ...

  9. 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.