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15 Cards in this Set

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  • Back
Allosteric Protein
protein whoe functional site can be altered by the binding of a small molecule at a non-overlapping site.
this latter site = allosteric site.
small molecule required for the biological activity of a protein.
Prosthetic group
a cofactor lightly bound to the protein.
disruption of conformation without breaking peptide bonds.
denaturation agents
heat, acid or base, alcohol.
grouping of 2 structural elements that occurs in many unrelated globular proteins.
structurally independent polypeptide units that have many of the characteristics of globular proteins.
amino acides as a function of hydrophobicity-hydrophobic
amino acids as a function of hydrophobicity-hydrophilic
one of the main roles of the proximal histidine residue at the binding site of hemoglobin is to -
bind to Fe directly.
what is special about the properties of proline that affect the conformation of proteins?
since it is a secondary amino acid with a ring structure, there is no rotation about the bond between the alpha-C and the N. thus it does not fit into an alpha-helical structure.
what is special about the properties of glycine such that it is always found in the B6(the sixth amino acid in the B helix) position in hemoglobin and myoglobin?
it has the smallest possible side group so the B and E helices can pass by close to one another.
which amino acid residue is generally not found in an alpha-helix?
which amino acid residue bonds directly to the iron atom in myoglobin?
which amino acid residue in hemoglobin binds directly to 2,3-bisphosphoglycerate (BPG)?
Lys or His