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33 Cards in this Set
- Front
- Back
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amino acid
- functions - basic structure |
- building blocks of proteins
- metabolism - neurotransmitters (glutamate, GABA, serotonin...) C + NH2 + COOH + H + side chain (R) |
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enantiomers
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mirror image forms of asymmetric carbons - L & D forms of carbs and amino acids. L for Living beings.
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zwitterion
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double ion.
Example: The COOH of an amino is acidic (gives off H) and the NH3 is basic (takes up H). |
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peptide bond
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A dehydration reaction links the carboxyl group of one amino acid to the amino group of another amino acid.
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dipeptide
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Two amino acids linked together by a peptide bond
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N-terminus
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The end of a peptide with the unbonded amino group, aminoterminus
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C-terminus
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The end of a peptide with the unbonded carboxyl group, carboxy terminus.
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oligopeptides
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polymers composed of a few amino acids; also peptides
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polypeptide
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protein; 100-1000+ amino acids
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primary structure
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The sequence of amino acids that make up a protein.
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secondary structure
- forms |
One portion of the polypeptide chain forms H bonds with another portion of the same polypeptide chain.
- Form alpha helix & beta sheets |
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tertiary structure
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3-D structure of a protein, and description of the precise position of all the atoms of all the amino acids of the protein.
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quaternary structure
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A description of all the subunits (proteins) within a functional unit (protein complex - like hemoglobin).
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fibrous proteins
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Insoluable proteins used to form hard or tough body structures (hair, skin, nails)
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globular proteins
- uses |
Water soluble proteins that take a roughly spherical shape. Non-repetitive amino-acid sequences
soft tissue, membrane proteins, enzymes |
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keratin
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A fiberous protein. Very rigid. A helix w/in a helix.
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collagen
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A tough fiberous protein that makes up connective tissue, tendon, bone and teeth.
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silk fibroin
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A fiberous protein formed from beta-pleated sheets that form acrachnid and insect silk.
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native structure
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the functional structure of a protein, dependent on its tertiary or 3D structure.
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denaturation
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The disruption of the native structure of a protein due to a change in pH or heat. Such a change is difficult to reverse.
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essential amino acids
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10 proteins we must eat, because we cannot make the one that are difficult to make - like bacteria and plants.
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protease
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Several enzymes that digest proteins through hydrolysis.
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endopeptidases
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Digestive enzymes that cleave peptide bonds in the middle of a protein molecule.
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aminopeptidases
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Enzymes that cleave one amino acid at a time from the N-terminus of a protein.
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carboxypeptidases
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Enzymes that cleave one amino acid at a time from the C-terminus.
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pepsin
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A major gastric enzyme that hydrolyses peptide bonds occuring between amino acids that have hydrophobic side chains. Protein -> shorter peptides.
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zymogen
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Inactive precursor of pepsin. Converted to pepsin by stomach acid and other pepsin molecules.
AKA pepsinogen. |
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trypsin
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Cleaves zymogens to active forms, and helps to digest dietary protein by hydrolyzing the peptide bonds that occur at the basic side chains of amino acids.
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chymotrypsin
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Hydrolyzes peptide bonds at aromatic amino acids.
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carboxypeptidase A & B
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Remove amino acids from the C-terminus of proteins and shorter peptides.
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elastase
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Hydrolyses peptide bonds in elastin (found in connective tissue)
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aminopeptidase N
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a membrane bound enzyme that further hydrolyses amino acids and short peptides in the enterocytes.
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side chain
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The -R group of an amino acid that defines it.
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