amino acid side chains

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  • Amino acid side chains may interact and bond in a number of ways.
  • Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding.
  • Also, amino acid side chain affinity for water was measured using vapor phases.
  • The first and third scales are derived from the physiochemical properties of the amino acid side chains.
  • Accurate packing of the amino acid side chains represents a separate problem in protein structure prediction.
  • This recognition was originally thought to primarily involve specific hydrogen-bonding interactions between amino-acid side chains and bases.
  • This same principle is the reason that hydrophobic amino acid side chains are oriented away from water, minimizing their interaction with water.
  • This is not actually the case, since the ensemble will be energy weighted due to interactions between amino acid side-chains, with lower-energy conformations being present more frequently.
  • These electrophilic groups react with amino acid side chains to form covalent adducts.
  • Although the ribbon diagram shows a hole in the protein's central core, the amino acid side chains are not shown in this representation.
  • VADAR reports accessible surface are values both for the entire amino acid residue and for the amino acid side chains.
  • Another interesting feature of such molecules and fabrics is that their amino-acid side chains point axially upwards from only one face; the opposite face has no side chains.
  • Amino acid side chains represent a broad range of functional groups and are sites of nonspecific reactivity during peptide synthesis.
  • Proteins are much more flexible in catalysis than RNA due to the existence of diverse amino acid side chains with distinct chemical characteristics.
  • Carboxyl groups are found on the C-terminal ends of proteins and on glutamate and aspartate amino acid side chains.
  • Shear motions involve a small sliding movement of domain interfaces, controlled by the amino acid side chains within the interface.
  • Other amino acid side chains alter the shape of this loop due to steric hindrance, and prevent proper NAD + binding.
  • The MG structure is believed to lack the close packing of amino acid side chains that characterize the native state (N) of a protein.
  • The charge of proteins is determined by the pKa of its amino acid side chains, and the terminal amino acid and carboxylic acid.
  • FDPB-based methods calculate the change in the pKa 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.
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