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33 Cards in this Set

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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)
enantiomers
mirror image forms of asymmetric carbons - L & D forms of carbs and amino acids. L for Living beings.
zwitterion
double ion.

Example: The COOH of an amino is acidic (gives off H) and the NH3 is basic (takes up H).
peptide bond
A dehydration reaction links the carboxyl group of one amino acid to the amino group of another amino acid.
dipeptide
Two amino acids linked together by a peptide bond
N-terminus
The end of a peptide with the unbonded amino group, aminoterminus
C-terminus
The end of a peptide with the unbonded carboxyl group, carboxy terminus.
oligopeptides
polymers composed of a few amino acids; also peptides
polypeptide
protein; 100-1000+ amino acids
primary structure
The sequence of amino acids that make up a protein.
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
tertiary structure
3-D structure of a protein, and description of the precise position of all the atoms of all the amino acids of the protein.
quaternary structure
A description of all the subunits (proteins) within a functional unit (protein complex - like hemoglobin).
fibrous proteins
Insoluable proteins used to form hard or tough body structures (hair, skin, nails)
globular proteins

- uses
Water soluble proteins that take a roughly spherical shape. Non-repetitive amino-acid sequences

soft tissue, membrane proteins, enzymes
keratin
A fiberous protein. Very rigid. A helix w/in a helix.
collagen
A tough fiberous protein that makes up connective tissue, tendon, bone and teeth.
silk fibroin
A fiberous protein formed from beta-pleated sheets that form acrachnid and insect silk.
native structure
the functional structure of a protein, dependent on its tertiary or 3D structure.
denaturation
The disruption of the native structure of a protein due to a change in pH or heat. Such a change is difficult to reverse.
essential amino acids
10 proteins we must eat, because we cannot make the one that are difficult to make - like bacteria and plants.
protease
Several enzymes that digest proteins through hydrolysis.
endopeptidases
Digestive enzymes that cleave peptide bonds in the middle of a protein molecule.
aminopeptidases
Enzymes that cleave one amino acid at a time from the N-terminus of a protein.
carboxypeptidases
Enzymes that cleave one amino acid at a time from the C-terminus.
pepsin
A major gastric enzyme that hydrolyses peptide bonds occuring between amino acids that have hydrophobic side chains. Protein -> shorter peptides.
zymogen
Inactive precursor of pepsin. Converted to pepsin by stomach acid and other pepsin molecules.

AKA pepsinogen.
trypsin
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.
chymotrypsin
Hydrolyzes peptide bonds at aromatic amino acids.
carboxypeptidase A & B
Remove amino acids from the C-terminus of proteins and shorter peptides.
elastase
Hydrolyses peptide bonds in elastin (found in connective tissue)
aminopeptidase N
a membrane bound enzyme that further hydrolyses amino acids and short peptides in the enterocytes.
side chain
The -R group of an amino acid that defines it.