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Transition metal amino acid complexes are a large family of coordination complexes containing the conjugate bases of the amino acids, the 2-aminocarboxylates. Amino acids are prevalent in nature, and all of them function as ligands toward the transition metals. [1] Not included in this article are complexes of the amides (including peptide) and ...
The presence of the metal ion allows metalloenzymes to perform functions such as redox reactions that cannot easily be performed by the limited set of functional groups found in amino acids. [16] The iron atom in most cytochromes is contained in a heme group. The differences between those cytochromes lies in the different side-chains.
The other amino acid residues, including non-natural amino acids and the peptide backbone have been shown to bind metal centers and provide donor groups. The research on metal-binding of peptides ranges from coordination of biometals (such as Calcium , Magnesium , Manganese , Zinc , Sodium , Potassium , and Iron ) to heavy metals (such as ...
The metal substitution in a natural metalloenzyme can result in a novel catalytic activity to the protein. The metal could be part of a prosthetic group (e.g., heme) or bound to amino acids; Amino acids with Lewis-basic properties in a hydrophobic pocket could interact with coordinatively unsaturated metal center.
Binding of metal ions via chelation is usually achieved via histidines or cysteines. In some cases this is a necessary part of their folding and maintenance of a tertiary structure. Alternatively, a metal-binding protein may maintain its structure without the metal (apo form) and bind it as a ligand (e.g. as part of metal homeostasis).
These chains are linear and unbranched, with each amino acid residue within the chain attached to two neighboring amino acids. In nature, the process of making proteins encoded by RNA genetic material is called translation and involves the step-by-step addition of amino acids to a growing protein chain by a ribozyme that is called a ribosome. [58]
The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)
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