Bio Exam Review

ATP Synthesis

The process of adding a phosphate group (Pi) to ADP to create ATP

ATP full name?

Adenosine Triphosphate

How does ATP become ADP + Pi?

The third phosphate is unstable in nature. When energy is needed, the third phosphate is broken resulting in ADP + energy

Phosphorylation

'Pi', the free phosphate from ATP attaches to other molecules in need of energy

Endergonic

If reactants store less energy in their bonds as products do, ENERGY IS ABSORBED

Exergonic

If reactants store more energy than the products make, ENERGY IS RELEASED

What reactions are endergonic?

Anabolic reactions like condensation/dehydration synthesis

What reactions are exergonic?

Catabolic reactions like hydrolysis

Catabolic reaction

large molecules are broken apart into smaller ones

Anabolic reactions

Builds up big molecules from smaller ones

Enzymes

Catalysts made out of protein

Catalysts

Speed up chemical reactions without taking part in it, reusable

Role of enzyme?

Allow molecules to come closer, assisting in reaction w/o need for heat. Lowers activation energy and makes transition state easier to obtain.

Active site

Groove substrates bond to on the enzyme

Substrate

reactant enzyme reacts with

Enzyme-substrate complex

overall attachment of enzyme and substrate

Induced-fit model (enzyme)

only the proper substrate can bind to a specific active site of an enzyme

enzyme inhibition

molecule (an inhibitor) that stops the proper function of an enzyme. how an enzyme stops working/functioning

competitive inhibitors

DIRECTLY COMPETES with substrates on ACTIVE SITE. many inhibitors, similar in shape to substrate flood the active site, blocking proper enzyme function

noncompetitive inhibitors

inhibitors attach to DIFFERENT SITE than active sites. the binding changes the shape of the enzyme and its active site, reducing enzyme function

allosteric regulation (enzymes)

controlling enzyme activity

allosteric sites

sites other than the active site on an enzyme

allosteric activator

binds to the allosteric site, stabilizing the ACTIVE FORM of the enzyme. (improves enzyme activity)

allosteric inhibitor

binds to the allosteric site, stabilizing the INACTIVE FORM of the enzyme. (decreases enzyme activity)

feedback inhibition

restricts the production of an enzyme itself, keeping its levels in check.

along the chain where a molecule is produced such as the end, the produced molecule can act as an allosteric inhibitor to one of the enzymes at the beginning of the sequence, slowing down the entire chain

the end product/end of the chain can slow down its own production

negative feedback

maintains balance by making changes to the system.

e.g. an enzyme has feedback inhibition to slow or stop the production of a molecule if it has too much of it

passive transport

follows concentration gradient, no energy is needed

forms of passive transport

simple diffusion and facilitated diffusion

simple diffusion

certain molecules such as gases, hydrophobic molecules, and small polar molecules can easily pass the cell membrane by following the concentration gradient

facilitated diffusion

special proteins such as CHANNEL PROTEINS, help bigger molecules pass

active transport

goes against the concentration gradient, requires energy supplied by ATP

bulk transport

large quantities or large substances moved in or out of the cell

endocytosis

large amount INTO cells from extracellular fluid

phagocytosis

bulk transport of SOLIDS

pinocytosis

bulk transport of LIQUIDS (extracellular fluid)

exocytosis

large amount OUT of the cytoplasm. materials moved out by SECRETORY VESICLE

4 types of macromolecules

carbohydrates, lipids, proteins, nucleic acids

monomers

small molecules

polymers

long chains of repeated monomers

what are carbohydrates?

common molecules found in living things that consist of C,H,O

function of carbohydrates

key for energy storage and structural support

what macromolecule is not a polymer?

lipids

subunit of carbohydrates

monosaccharides (single sugar units) such as glucose

disaccharides

two single sugars put together

oligosaccharides

small amount of simple sugars, 2 or 3

polysaccharide

hundred to thousands of monosaccharide subunits

what bond holds simple sugars/monosaccharides together?

glycosidic linkages

what are lipids?

molecules made of C, H, O. have lots of C-H single bonds making them non-polar and hydrophobic.

hydrophobic

water fearing. the tendency for NONPOLAR molecules to exclude/not mix with water

hydrophilic

water-loving. POLAR molecules and IONIC substances affinity for water (dissolve in water)

subunits of lipid

glycerol and fatty acid molecules (3)

function of lipids

store energy, build membranes and other cell parts, act as chemical signalling molecules

what does 1 glycerol + 3 fatty acids make?

triglyceride, the most common fat

macromolecules

large organic molecules sometimes composed of repeating subunits

monounsaturated fatty acids

• only one carbon double bond

• straight-chain shape

• solid at room temp

• can stack tightly

polyunsaturated

• two or more carbon double bonds

• bent shape

• liquid at room temp

• cannot stack tightly

protein function

used for structure and function, molecules that make cellular activities take place

subunit of proteins?

amino acids

what are amino acids composed of?

An amino group, a carboxyl group, and an 'R" side chain group which can be 20 different groups

what are proteins composed of?

composed of repeating amino acids, that become peptides and then polypeptides

what bond forms between amino acids?

peptide bond

primary structure of protein

sequence of amino acids, straight-line

secondary structure of protein

coils (alpha helixes) OR folds (beta-pleated sheets)

tertiary structure of protein

coils AND folds. some R-group attract each other

quaternary structure of protein

two or more separate proteins come together for a specific function. held together by h-bonds, ion/dipole attractions, or disulphide links

what are nucleic acids?

informational molecules

function of nucleic acids?

store hereditary information, can produce identical copies of themselves

subunit of nucleic acids?

nucleotides (phosphate group, pentose sugar, nitrogenous base)

what bond attaches the nitrogenous base to the 1' carbon

glycosyl bond

what bond attaches the phosphate group to the 5' carbon

ester bond - phosphodiester bond

functional group

reactive cluster of atoms attached to the carbon backbone of organic materials

significance of functional groups?

functional groups give biological molecules their specific chemical properties; how they react, what they bond with and what functions they preform

stages of cellular respiration

1. glycolysis

2. pyruvate oxidation

3. krebs cycle

4. electron transport chain (ETC) + chemiosmosis

stages of photosynthesis

1. light-dependent reactions: non-cyclic and cyclic (chemiosmosis)

2. light-independent reactions: calvin cycle

where does glycolysis occur?

outside mitochondria, cytosol

where does pyruvate oxidation occur?

matrix

where does krebs cycle occur?

matrix

where do the ETC and chemiosmosis occur?

inner membrane

where do light dependent reactions, non-cyclic and cyclic occur?

thylakoid membrane

where do light independent reactions, calvin cycle occur?

stroma (fluid of chloroplasts)