1. Properties of Water

-water is a POLAR molecule (hydrogen=slightly positive; oxygen=slightly negative)

why? water has an unequal sharing of electrons between the atoms

2. Hydrogen Bonding

definition: molecules attract due to partial charges

this type of bonding has to occur with hydrogen (+) and another molecule (-)

the attraction is usually weak and not as strong as a covalent bond

water is an example of this- if water did not have a hydrogen bond, it would not be a liquid and have the capability to sustain life

3. Types of Macromolecules

Amino Acids:

the fundamental molecule that serves as the building blocks for proteins

monomers that makeup proteins

Carbohydrates:

consisting of carbon, hydrogen, and oxygen atoms

an organic compound such as sugar or starch, and is used to store energy

Nucleic Acids:

typically DNA and RNA

must have a phosphate group, a sugar, and a nitrogenous base

4. Monomers/Polymers in Monomerization and Polymerization

Dehydration Synthesis:

takes water out of the molecule

Hydrolysis:

water is being put into the molecule

water is “shoved” in and breaks the molecule

opposite of synthesis

ex: sugar-building carbohydrates

5. Cell Membrane

definition: separates and protects the interior of the cell from the outside environment

Made up of two layers:

phospholipid and the polar ends of molecules

phospholipids have a hydrophilic head and a hydrophobic tail

because of this polarity, the membrane forms in a way that water is not near the tails

the structure is constantly moving

What can get into the cell?

lipid molecules

small nonpolar molecules- that way they can fit through

when the molecules trying to pass through are too big or are polar, they have to go through protein channels which allow more molecules in (passive transport)

Active Transport: uses energy to pump things out of the cell

6. Amino Acid Structure

the side groups (R group) are in green in the picture above

How do you tell the properties of the side group?

you can tell based on the individual elements in the group and their electronegativity

polar and non-polar element

7. Four Types of Protein Levels

Primary Structure:

This is the 1st layer of the protein

it serves as the building block for the protein to form

the “sequence” of amino acids linked together to form the polypeptide chain in a linear sequence

Tertiary Structure:

this is the overall 3-D structure of the polypeptide chain

it is stabilized by outside polar hydrophilic and hydrophobic and ionic bond interactions

Quaternary Structure

the association of several protein chains in a closely packed unit

What happens when one of the amino acids in the sequence is removed?

The structure has to fold in a new way because of the properties of the amino acids. Some of them don’t like being next to each other and have to fold in a way so that they are not next to each other.

hydrophobic, hydrophilic, acid, and base

What if you change one of the amino acids for the same one?

nothing changes

8. Water Interacting with Amino Acids

main idea: it creates the tertiary structure of the protein structure

location in the protein: in the center because they are hydrophobic

cysteine chains from covalent bonds with each other when exposed to oxygen

9. Primary Level is Responsible for Tertiary Level

each side chain has amino acids in a specific order in the primary level of protein and ordered in a certain way

depending on the order of the amino acids, the rules for each amino acid still apply, so the chain has to fold in a different way to meet the requirements for amino acids

everything will change the protein structure unless you take out the same exact amino acid and replace it with the same one

10. Enzymes and How They Work

what is an enzyme?

a biological catalyst

speeds up the rate of a specific chemical reaction in a cell

is not destroyed in the reaction and can be used over and over again

they function best at a specific temperature, pH, and salt concentration- if it is not perfect, they won’t work

What happens when you don’t have enzymes?

activation energy goes up because the enzyme is not there to speed up the process so it has to work harder to do the same thing

11. Enzyme Processes

Induced Fit Model

The substrate binds to the active site which is where everything happens and slightly alters the shape of the active site. The enzyme puts strain on the substrate causing it to break which creates the product. Everything in the cell happens rapidly.

Passive Transport:

no energy is being used

high to low concentration

Facilitated Diffusion

When a molecule is too big to pass through the membrane, it can pass through a protein channel

type of passive transport

Active Transport: (Audie’s Favorite type of transport)

uses energy with protein channels to get things through the membrane of a cell

12. What Affects Enzymes in a Cell?

enzymes are picky (just like Audie) ♥️so they only like a specific environment

they like to have a specific pH, temperature, and concentration

enzymes bind to the reactant molecules and change their shape

lowers the activation energy 👍🏼

🤓

What happens when you don’t have enzymes?

the reaction in cells would not occur or run too slowly to keep organisms alive

Why do enzymes work at the rate they do?

If enzymes worked too quickly, too much heat energy is created making the process inefficient

when it occurs slowly and carefully, it can do its specific job better and more efficiently

13. Competitive and Noncompetitive Inhibition and Feedback Inhibition

Competitive:

the inhibitor resembles the substrate, taking its place and binding to the active site of an enzyme

example: caffeine; it doesn’t give you energy just makes you not know that you are tired

Noncompetitive (Allosteric)

inhibitor molecule binds to the enzyme in a location other than the active site known as the allosteric site

prevents the substrate to bind to the active site

changes the shape of the active site reduces the enzyme activity

Feedback Inhibition:

occurs when the end product of a reaction interferes with the enzyme that helped produce it. The inhibitor does this by binding to a second active binding site that's different from the one attached to the initial reactant. The enzyme then changes its shape and can't catalyze the reaction anymore.

Other Random Questions:

Where does matter and energy come from and where do they go?

all living organisms require energy

if something has energy, it can cause change

energy is never created or destroyed instead it is transferred and transformed