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  2. Protein dynamics - Wikipedia

    en.wikipedia.org/wiki/Protein_dynamics

    A network of alternative conformations in catalase (Protein Data Bank code: 1gwe) with diverse properties. Multiple phenomena define the network: van der Waals interactions (blue dots and line segments) between sidechains, a hydrogen bond (dotted green line) through a partial-occupancy water (brown), coupling through the locally mobile backbone (black), and perhaps electrostatic forces between ...

  3. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The primary structure of a protein, its linear amino-acid sequence, determines its native conformation. [11] The specific amino acid residues and their position in the polypeptide chain are the determining factors for which portions of the protein fold closely together and form its three-dimensional conformation.

  4. Protein adsorption - Wikipedia

    en.wikipedia.org/wiki/Protein_adsorption

    It is a valuable tool for measuring protein-protein and protein-surface interaction. However, the limiting factor of many AFM studies is that imaging is often performed after drying the surface which might affect protein folding and the structure of the protein layer. Moreover, the cantilever tip can dislodge a protein or corrugate the protein ...

  5. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    FDPB-based methods calculate the change in the pK a value of an amino acid side chain when that side chain is moved from a hypothetical fully solvated state to its position in the protein. To perform such a calculation, one needs theoretical methods that can calculate the effect of the protein interior on a p K a value, and knowledge of the pKa ...

  6. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Other factors suspected to affect degradation rate include the rate deamination of glutamine and asparagine and oxidation of cystein, histidine, and methionine, the absence of stabilizing ligands, the presence of attached carbohydrate or phosphate groups, the presence of free α-amino group, the negative charge of protein, and the flexibility ...

  7. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    Structure stabilized by the formation of weak bonds between amino acid side chains - Determined by the folding of the polypeptide chain on itself (nonpolar residues are located inside the protein, while polar residues are mainly located outside) - Envelopment of the protein brings the protein closer and relates a-to located in distant regions ...

  8. How Much Protein Do You Need To Eat Every Day? - AOL

    www.aol.com/lifestyle/much-protein-eat-every-day...

    One of the biggest factors affecting protein needs is activity level. If you love busting out weight reps at the gym most days of the week, you likely need more protein compared to someone who is ...

  9. Post-translational modification - Wikipedia

    en.wikipedia.org/wiki/Post-translational...

    [2] Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called glycosylation, which can promote protein folding and improve stability as well as serving regulatory functions. Attachment of lipid molecules, known as lipidation, often targets a protein or part of a protein attached to the cell ...

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