Unit 1 Bio Test IB HL

the sum of all chemical reactions in a cell or organis

metabolism

the ability to do work (move an object against an opposing force)

energy

series of reactions involved in metabolism processes

metabolic pathways

what type of metabolic pathways can there be

linear or cyclic

what do u cells use to control metabolic reactions

enzymes

whats an example of a linear pathway

glycolysis (part of respiration) l

whats an example of cyclic pathway

urea cycle

anabolism

join small molecules, make big ones NEED ENERGY

Catabolism

Break large molecule, make small RELEASE ENERGY

whats an example of anabolic reaction

dehydration synthesis

whats an example of catabolic reaction

hydrolysis

Enzymes Biological catalysts

speed up chem reactions without being consumed

what type of proteins are enzymes

globular proteins

examples of enzymes

lactase, amylase

active site

where an enzyme specifically binds the substract

substrate

reactant (starting substances)

what is this

lock and key hypothesis

induced fit hypothesis

enzymes and substrates change to slightly better fit

what hypothesis is this

induced fit

collision theory

E and S collide in correct orientation for reaction

when will there be more collisions

high temps and higher concentration w

when will there be fewer collisions

low concentration and low temp

what is DNA replication an example of (idea)

that some large substrate molecules need enzyme to move

what is cell membrane an example of

that some enzymes are immbolilized

what is the problem with denatured active sites

prevents substrate from binding

what 4 factors effect enzyme activity

1. enzyme concentration

2. substrate concentration

3. temperature

4. pH

what type of increase is enzyme concentration (assuming high of substrate)

linear increase assuming high of substrates and more active sites

what type of increase would substrate concentration cause

initally increase (PLATEAU) , more substrate = more likely to collide with enzymes

plateau

all enzyme active sites are taken

what happens when pH is further from optimal

active site is denatured more

why temp matter?

less kinetic energy, fewer collisions

2 things to measure reaction rate

1. fixed time

2. time of completion

First Law of Thermodynamics

energy not destroyed or created, just converted

activation energy (Ea)

minimum amount to break bonds in reactants T

transition state

intermediate condition where bonds in reactants are breaking and bonds in products are forming

what type of reaction

exothermic

what reaction energy

endothermic

after enzymes bind to reactant molecules what hpappens to transition state

lower the energy

what does enzyme lower activation energy mean

less energy to start reaction, more likely reaction will occur

what type of reaction

exergonic

what type of reaction

endergonic reaction

2 ways enzymes lower activation energy

1. bring molecules together in the correct orientation

2. change shape of substrate

heat is a byproduct of…

metabolism

what is brown adipose tissue

humans produce more heat during respiration and less ATP

allosteric site

binding site for regulatory molecules

allosteric regulation

enzyme changes shape when allosteric molecule bound

what does the allosteric site do

control when enzyme is active

what may the allosteric regulation do

may allow or prevent substrate from binding

what is.a competitive enzyme inhibition

inhibitor binds to active sit and blocks substrate

what is a noncompetitive enzyme inhibition

inhibitor binds to allosteric site

which inhibitor has a higher inital rate of reaction

competitive inhibitor

allosteric (non-competitive inhibition)

end product of a pathway inhibits an earlier enzyme

negative feedback

controls levels within a set range like body temp

mechanism-based inhibition

inhibitor is permanentaly bound to active site and enzyme is inactivated

penicillin

blocks active sit on transpeptidase enzyme in bacteria

what happens to cells ways in penicillin

cells walls cannot be built properly, cell bursts

what carries genetic information

is dna deoxyribonucleic acid

whats nitrogenous base + pentose sugar +phosphate group

nucleotide

whats the difference between DNA vs RNA

DNA has one less oxygen on carbon 2

whats the difference between purines and pyriidines

purines = 2 rings
pyrmidiries = 1 ring

at the groupchat mmenoic

AT GC

ACTG vs ACUG

DNA vs RNA

whats the bond between nucleotides (sugar and phosphorus)

phosphodiester

what is the special thing about DNA structure

its double stranded, so they’re anti parallel, so flipped

what carbons does. the dehydration synthesis/condensation join at

C5 (phosphorus) and C3 (OH)

what type of bond is a phosphodiester

a strong covalent one

what type of bond is the hydrogen bond

weak

main difference between DNA and RNA

DNA = genetic info

RNA is the process of transcribing genetic info from DNA into proteins

how else is the DNA double stranded helix called

complementary base pairing

what type of strand is RNA

single

type of enzymatic protein

acceleration of chemical reactions

structural proteins

collagen & elastin, keratin (hair and nails)

transport proteins

transport of other substaces

hormonal proteins

cellular communication

contractile

movement

defensive

protect against disease

what 4 type of amino acids are there

1. nonpolar

2. polar

3. charged/acidic

4. charged/basic

LUCA

last universal common ancestor

whats the bond in the sulfhydye group

disulfide bridge

primary structure

sequence of amino acids joined by polypeptides

whats the possibilites of amino acids

20^n

whats the H2N- called

N-terminus

whats the carboxylic acid side called

c terminus

secondary structure

hydroge bonding between amino acid backbone

whats the 2 important things in 2nd structure

alpha helix and beated sheets

tertiary structure

interactions between side chains (R groups)

what type of tertiary structures are there (4)

1. charged ionic bonds

2. polar hydrogen bonds

3. non polar hydrophobic

4. disulfide bridge (cysteine)

where is the hydrophilic interaction (outside or inside)

the outside (exposed to cytoplasm/water)

where is the hydrophobic interaction (outside or inside)

inside (amino acids fold into middle)

whats the thing about phospholipids

polar on the outsides and non polar on the inside

quaternary structure

two or more folded polypeptides come together to make a functional proteins

how can polypeptides may be held together together

ionic bonds, hydrogen bonds, etc

non conjugated protein

only poplypetide (insulin and collagen)

conjugated proteins

one or more non polypeptide unit (hemoglobin has heme)

example of globular protein

hemoglobin or insulin

example of fibrous protein

collagen

what causes denaturation

heat and pH changes

what is denaturation

protein unfolds, breaks 2nd, 3rd or 4th structure p

proteome

all proteins produced by cell, tissue or organism

proteomics

study of which proteins are active in certain cell at certain time