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13 Cards in this Set
- Front
- Back
what makes one amino acid different from another amino acid |
The R (residue) group differs with each amino acid. |
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What is the pKa of an amino acid |
The pKa is the pH at the inflection point where the slope is very shallow. pKa is the pH where is concentration of the deprotonated form equals the concentration of the protonated form. At the pKa, buffering capacity is optimal and thus changes in the pH due to the addition of acids and bases are resisted - a shallow slope. |
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zwitterion |
a zwitterion is a form of molecule which carries both a positive an negative charge, it occurs at a pH value between the pKa values of the ionizable group. |
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What is the isoelectric point |
pH value at which the number of positive charges equals the number of negative charges. tied to the zwitterion being in the middle. |
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polypeptide |
a polypeptide is a chain made of more than 50 amino acids. |
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oligopeptide |
chain made of 3-50 amino acids |
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Primary structure |
the covalent linear structure of the protein that is specified by its amino acid sequence as determined by the genetic code. |
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Secondary structure |
localized regular, repitive folding patterns; alpha helix and beta pleated sheets . |
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Tertiary structure |
refers to the overall 3D folding pattern of the polypeptide; creates binding sites and situates R groups in the appropriate environment. |
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Quaternary structure |
formed by the interactions between different polypeptide chains, known as subunits; results in increased protein structure and the possibility of cooperativity for ilgand binding. |
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ligand |
molecule that binds to a binding site on a protein. |
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prosthetic group |
a coenzyme or metal ion that is very tightly or even covalently bound to the enzyme protein is called the prosthetic group. in absence of the prosthetic group, the polypeptide component is known as an apoprotein; in its presence, known as a holoprotein. |
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2 ways proteins can be denatured |
acid and heat |