Ch. 5: Macromolecules Flashcards
Hydrogenation
converting unsaturated fats to saturated fats by adding hydrogen. Increases shelf life
Alpha glucose
Starch. Helix. Can be broken down. Plant cells energy.
Beta glucose
Cellulose. Straight. Can’t be broken down. Plant cells structure.
Steroids
A lipid. A carbon skeleton consisting of four fused rings. EX sex hormones.
Cholesterol
Essential steroid, a component in animal cell membranes
Protein
A functional protein consists of one or more polypeptides, twisted, folded and coiled into a unique shape
Primary structure
the sequence of amino acids in a protein, is like the order of letters in a long word. The chain. Determined by your DNA
A slight change in primary structure can affect a protein’s structure and therefore its ability to function.
Secondary Structure
Coils and folds as a result of hydrogen bonds between repeating constituents of the polypeptide backbone. Typically are coiled, alpha helix, or are folded and called beta pleated sheets.
3Tertiary structure
When R groups interact. Could be final protein.
Quaternary structure
two or more polypeptide chains form one macromolecule.
Renaturation
from denaturation, a protein can sometimes return to original shape thru renaturation.
Chaperonins
protein molecules that assist in the proper folding of other proteins.
gene
The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene, made by DNA.
nucleotide structure
consists of a nitrogenous base, a pentose sugar (5C’s) and a phosphate group.
Two families of nitrogenus base:
Pyrimidines
Purines
Pyrimidines (cytosine, thymine, and uracil) have a single six- membered ring
Purines (adenine and guanine) have a six- membered ring fused to a five-membered ring