Biochemistry Flashcards
_______________
- fundamental subunit of polypeptides/proteins
Amino acid
(AA)
There are ____ amino acids that are coded for by the DNA & there are ____ essential amino acids and ____ nonessential amino acids
20
9
11
Amino Acid Structure includes :
____________ bonded to a hydrogen
____________ group
____________ group
____________ group
Central a-carbon bonded to a hydrogen
Amine group (-NH2)
Carboxyl group (-COOH)
Variable functional group (R-group)
All amino acids are chiral except ____________
Glycine
_______________
- 4 different distinct groups bound to an α-Carbon resulting in non-superimposable mirror-images
- a form of isomer with different configuration around a chiral center (forms 2 isomers)
Enantiomers
Amino acids form __________ at low pH
Amino acids form __________ at high pH
Amino acids form __________ at intermediate pH
Cations
Anions
Neutral zwitterions (contains both positive and negative electrical charges, but the net charge on the molecule is zero COO- & NH3+)
R-group chemical properties :
____________ - aliphatic or aromatic
____________ - pH neutral, acidic, alkaline, 3 with sulfur, or selenium
Non-polar
Polar
____________
- amino acids form peptide bonds by dehydration synthesis between the amino group of 1 amino acid & the carboxyl group of another amino acid
Polypeptide synthesis
Polypeptide synthesis is facilitated by ribosomes during ____________ of mRNA
translation
Proteins are composed of 1 or more long ____________ molecules
polypeptide
Other bonds formed in the synthesis & activation of proteins include __________ linkages between cysteine R-groups and __________ bonds between polar R-groups
Disulfide linkages
Hydrogen Bonds
In protein digestion, the protease or peptidase enzymes break peptide bonds via ____________
Hydrolysis
____________ structure
- actual sequence of amino acids in the protein due to peptide bonds
Primary structure
____________ structure
- 2 common configurations
- a-helix & B-pleated sheet are due to Hydrogen bonds between amine hydrogens and carbonyl oxygen of amino acids
- especially prevalent in fibrous structural proteins
Secondary structure
____________ structure
- 3D shape of entire polypeptide due to interaction among hydrophobic R-groups & hydrophilic R-groups, hydrogen bonds, ionic bonds, & disulfide bridges between cysteine R-groups
Tertiary structure
Structural proteins usually have ________ tertiary structures
Fibrous
Enzymes usually have ________ tertiary structures
Globular
____________ structures
- 2 or more polypeptides combine to form a functional protein or incorporation of ligands
- ex : Fe containing heme groups of hemoglobin
Quaternary structures
Long sequences of (non-polar OR polar) amino acids are found in membrane-bound proteins or membrane-embedded proteins & attach protein to lipid bilayer or folded into the interior to stabilize the 3D structure of proteins dissolved in water
Non-polar
____________
- disruption of protein/polypeptide folding & activity by changes in pH, Temperature, or presence of hydrophobic solvents
Denaturation
____________
- correct refolding of denatured protein
Renaturation
____________
- dissolved proteins are surrounded by water molecules oriented according to the charges of the amino acids in that particular surface of the folded protein
- have properties key to binding of substrates to protein active sites
Solvation layer
____________
- proteins are forced by electric current to pass through a medium that sorts molecules by size, charge, and/or other chemical properties
Electrophoresis
__________________
- proteins have unique combinations of R-groups charged positive or negative
- at a specific pH then a particular protein acquires neutral charge (therefore stops moving due to no electromagnetic field force)
- proteins then separated along a pH gradient gel with cathode & anode charges at either end
Isoelectric focusing