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15 Cards in this Set
- Front
- Back
Allosteric Protein
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protein whoe functional site can be altered by the binding of a small molecule at a non-overlapping site.
this latter site = allosteric site. |
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Cofactor
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small molecule required for the biological activity of a protein.
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Prosthetic group
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a cofactor lightly bound to the protein.
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denaturation
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disruption of conformation without breaking peptide bonds.
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denaturation agents
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heat, acid or base, alcohol.
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motif
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grouping of 2 structural elements that occurs in many unrelated globular proteins.
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domain
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structurally independent polypeptide units that have many of the characteristics of globular proteins.
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amino acides as a function of hydrophobicity-hydrophobic
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F,I,L,M,V
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amino acids as a function of hydrophobicity-hydrophilic
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D,R,K,E,N,H,Q
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one of the main roles of the proximal histidine residue at the binding site of hemoglobin is to -
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bind to Fe directly.
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what is special about the properties of proline that affect the conformation of proteins?
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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.
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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?
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it has the smallest possible side group so the B and E helices can pass by close to one another.
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which amino acid residue is generally not found in an alpha-helix?
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Pro
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which amino acid residue bonds directly to the iron atom in myoglobin?
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His
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which amino acid residue in hemoglobin binds directly to 2,3-bisphosphoglycerate (BPG)?
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Lys or His
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