attracts/wants a lot of electrons (ex. h20; O2's electronegativity leads to an unequal sharing of electrons
between hydrogen and oxygen; aka it's a polar molecule) - Answers Electronegativity
Very weak, but if you have enough of them. they can be significant (ex. a lot of water molecules can lead
up to surface tension) - Answers Hydrogen Bonds
When electrons from 1 atom are TRANSFERRED to another (ex. NaCl, Na loses an e-, now it is positively
charged, and Cl accepts the e-, so it becomes neg. charged) - Answers Ionic Bonds
Same molecular formula but DIFFERENT structure (3 types):
1. structual isomers- differ in covalent arrangement of atoms
2. Geometric Isomers- basically arranged identically, atoms arranged differently
3. Stereoisomers- molecules are mirror images of each other - Answers Isomers
OH = alcohol
N= amine
P = Phosphate
S = Thiol - Answers Functional Groups
Trioses (3 carbons): glyceraldehyde
Pentoses (5 carbons): ribose and deoxyribose (in DNA and RNA)
Hexoses (6 carbons): glucose, fructose, and galactose; the only sugar that can be absorbed by the body
Polar/hydrophilic, freely soluble in blood plasma(water). - Answers Carbohydrates
Take a H20 out and the sugar molecules band (this is aka a dehydration synthesis/condensation). This is
how disaccharides are formed - Answers Glycosidic Linkage
Add water to break sugars apart - Answers Hydrolysis
we can make nonessential; we need to eat essential amino acids - Answers Nonessential amino acids vs
essential Amino acids
SIMPLEST possible amino acid because it has only one hydrogen as functional group - Answers Glycine
(Gly)
has SULFUR, that can work as super glue - Answers Cysteine (Cys)
, the most important amino acid because it is the FIRST amino acid attached in protein. - Answers
Methionine (Met)
Formed through condensation dehydration (take H20 out) between amino group and carboxyl group. -
Answers Peptide bonds
Primary Structure: many different peptide bonds containing amino acid sequences
Secondary Structure:
Α helix
𝛃 Pleated Sheet
Tertiary Structure: crystallized form of three bonded secondary structures
Quaternary Structure: 4 bonded subunits of polypeptides - Answers 4 levels of Proteins
loss of tertiary structure (functioning protein); usually happens because of antibodys, temperature etc -
Answers Denaturation
Not the best energy storage, very inefficient in terms of space.
It stores energy quick, but takes up a lot of space - Answers Glycogen, good or bad at storing energy?
and why?
CANT DIGEST!!! Animals need bacteria (e.coli) to help them breakdown the sugar so they can absorb it.
ex. cows chews food, throws it up in its mouth, chews it again
bunnies eat poop - Answers Cellulose
good for storage because it takes up a LOT less space than glycogen.
NONPOLAR, does not dissolve in water/blood - Answers Lipids
(No carbon double bonds): solid at room temp - Answers Saturated Fats
One or more double bonds - Answers Unsaturated fats
can be used for energy but has drawbacks:
toxic for the body!! leads to ketosis and ketoacidosis (change in blood pH, could be fatal) - Answers
Ketones
cholesterol is used to make testosterone/estrogen; VERY IMPORTANT - Answers Fats (uses for
hormones)