Ch. 3 Biologically Important Molecules Flashcards
amino acids
The building blocks (monomers) of proteins. There are 20 different ones.
cholesterol
A large, ring-shaped lipid found in cell membranes. Is the precursor for steroid hormones, and is used to manufacture bile salts.
lipoproteins
Large conglomerations of protein, fats, and cholesterol that transport lipids in the bloodstream.
phospholipid
The primary membrane lipid. They consist of a glycerol molecule esterified to tow fatty acid chains and a phosphate molecule. Additional, highly hydrophilic groups are attached to the phosphate, making this moleucle extremely amphipathic.
proteins
Biological macromolecules that act as enzymes, hormones, receptors, channels, transporters, antibodies, and support structures inside and outside cells
peptide bonds
covalent bonds between amino acids in proteins, link amino acids into polypeptide chains
disulfide bridges
covalent bonds between amino acids in proteins, link amino acids between cysteine R-groups
backbone of the polypeptide
N-C-C-N-C-C
residue
an individual amino acid when it is part of a polypeptide chain
Proteolysis (proteolytic clevage)
hydrolysis of a protein by another protein
Proteolytic enzyme (protease)
protein that does the cutting in hydrolysis of a protein
denatured
improperly folded proteins, makes proteins non-functional
Denaturation
disruption of a protein’s shape without breaking peptide bonds
Primary Structure (sequence)
linear ordering of amino acid residues
Secondary Structure (hydrogen bonds between backbone groups)
refers to the initial folding of a polypeptide chain into shapes stabilized by hydrogen bonds between NH and CO groups. 2 most common structures: alpha-helix and beta-pleated sheet
Alpha Helix
secondary structure
parallel beta-pleated sheet
secondary structure, adjacent polypeptide strands running in the same direction
anti-parallel beta-pleated sheet
secondary structure, adjacent polypeptide strands run in the opposite directions
Tertiary Structure (Hydrophobic/Hydrophilic Interactions)
interactions between amino acid residues located more distantly from each other in the polypeptide chain. Hydrophobic R-groups tend to fold into the interior of the protein, away from the solvent, and hydrophilic R-groups tend to be exposed to water on the surface of the protein.
Quaternary Structure (Various Bonds Between Separate Chains)
Describes interactions betweens polypeptide subunits.
Subunit
single polypeptide chain that is part of a large complex containing many subunits (a mulitsubunit complex)
monosaccharide (simple sugar)
single carbohydrate molecule, general chemical formula: C(n)H(2n)O(n)
glycosidic linkage
bond between 2 sugar molecules
Glycogen
energy storage carbohydrate in animals and is composed of thousands of glucose units