Bio 1000 Final Exam

AHHHHHH

what are the 5 basic characteristic of life in all organisms?

1. evolution

2. energy

3. genetic information

4. reproduction

5. made of cells

what is the theory of evolution?

traits of a population change over time due to different

• survival of the fittest

all species come from a common ancestor

what is cell theory

everything is made from cells

all cells come from preexisting cells

what is needed in order for evolution to occur

variation in a population where less common traits become common because it is advantageous for that organism in their environment

what is a nucleoid?

where a singular circular chromosome is located. found in bacteria

what protein helps with binary fission

FtsZ protein

• very similar to the contractile ring in euks

when might a plasmid be beneficial

provide the organism (mainly bacteria) with additional traits that may or may not be beneficial to surviving in certain environments

what protein keeps the cell shape of a bacterial cell?

MreB

how does the bacterial plasma membrane differ from a eukaryotic cell membrane?

• has ETC for making ATP because they don’t have mitochondria

• in cyanobacteria (photosynthetic bacteria) will make glucose because they don’t have chloroplasts

what are bacterial cell walls made out of?

they are peptidoglycan

• peptide cross bridge and carbohydrate backbone

what are the different types of cell walls for bacteria?

gram positive: single thick peptidoglycan layer

• stains purple

gram negative: thing peptidoglycan layer surrounded by the outer membrane

• stains pink

what do some bacteria have to protect their cell membrane from things like antibodies or lysozyme?

glycocalyx

• slime layer: loose and hydrated

• capsule layer: tight, less hydrated but more protective than slime layer

what is the difference between flagella and fimbriae?

flagella: long whip like structures, used for moving around

fimbriae: short hair like projections, used for sticking to surfaces (pili)

• both made out of different proteins

how are archaea unique from both bacteria and eukaryotes?

extremophiles

3 major differences from euks and proks

1. euks have a nucleus and membrane bound organelles

2. euks are much larger

3. euks have linear DNA, proks have circular DNA

primary protein structure

linear chain of amino acids held together by peptide bonds

secondary protein structure

alpha helices or beta pleated sheets, held together by hydrogen bonds

tertiary protein structure

lots of folding and R group interactions

• ionic bonds

• hydrogen bonding

• hydrophobic interactions

• disulfide bridges

quaternary proteins

multiple tertiary proteins come together to make one protein complex. still has R group interactions

• Hydrogen bonds

• ionic bonds

• hydrophobic interactions

• disulfide bridges

how is a protein able to be flexible?

the level of bonding varies in a protein

• would have less flexible regions where there are more disulfide bridges

carbs form what three structures?

1. monosaccharides

2. disaccharides

3. polysaccharides

what are nucleotides made of?

1. nitrogenous base

2. pentose sugar

   1. phosphate group

what are the 6 organelles in the endomembrane system

1. nuclear envelope

2. SER/RER

3. gogli

4. vesicles

5. lysosomes

6. vacuoles

4 main purposes of the endomembrane system

1. proteins (synthesis, mods, transport)

2. lipid synthesis

3. detoxification

4. transportation and breakdown of large biomolecule-containing particles

smooth ER

lipid synthesis

golgi apparatus

modification of proteins

• has cisternae - flattened sacs that help with the flow of processing proteins

lysosome

recycling center

• autophagy - when a damaged organelle is packed in a vesicle and sent to the lysosome

vacuoles

temporary storage for nutrients and waste

rough ER

• protein synthesis (due to the ribosomes attached to it)

• transportation to the golgi for final protein mods

• protein folding and modification

what are the two things that protect the nucleus?

1. nuclear lamina - made of lamins and is under the nuclear envelope

2. nuclear envelope - double membrane and has nuclear pores

endomembrane system evolution

1. started with ancestor that just had chromosome and plasma membrane

2. infoldings of plasma membrane surrounded chromosome

3. form organelles of endoplasmic reticulum

how are RNA made?

in the nucleus at the nucleolus

what is the route of a newly synthesized protein

RER → vesicle → cis golgi → trans golgi → secretory vesicle → plasma membrane → exocytosis

what is essential to targeting a protein to the ER? (first step)

the ribosome has to synthesize an ER signal sequence so the protein knows to go to the ER

what combination of parts allow the binding to an SRP receptor at the ER

ribosome + signal sequence + SRP

translocon channel at the ER

where protein synthesis continues through

why did the host cell and bacterium cell stay inseparable?

formed a symbiotic relationship where the bacteria provides energy and the host cell provides protection

what is the evidence of endosymbiosis

• the mitochondria/chloroplasts have their own transcription and translation machinery

• contain their own DNA

purpose of cytoskeleton

gives cell strength and shape

• helps with intracellular transport

what are the two types of cytoskeletal filaments that are dynamic

actin (mircofilament) and microtubule

how do actin filaments aid in amoeboid movement

they gather in an ameoba at the leading edge (direction it wants to move) and then moves the whole cell

main function of intermediate filaments

provide mechanical strength

how are tubulin dimers involved in microtubules

polymerize: adding tubulin dimers

depolymerize: removing tubulin dimers

what is muscle contraction caused by

actin and myosin

• myosin walks towards actin plus end and pushes it back

kinesin vs dyenin

they both walk along the microtubule track carrying a vesicle

• kinesin walks towards plus end

• dynein walks towards minus end

how is dynein involved in the microtubule 9+2 complex for flagellar and ciliary movement

dynein that are between the doublets makes microtubules slide but because of their bonds it causes the microtubules to bend

when a cell’s diameter gets bigger what is the risk/problem?

the volume of the cell increases more than the surface area

• the cell won’t be able to facilitate movement of what comes in and out efficiently enough

how do euks compensate for having a low volume to SA ratio? there are total 4 things

1. compartmentalization

2. being thin

3. using folds with villi

4. specialized structures like the mitochondria

catabolic vs anabolic reactions

catabolic: breaking bonds, spontaneous, releases energy (exergonic)

anabolic: building bonds, non-spontaneous, uses energy

1st and 2nd law of thermodynamics

1st law: energy cannot be created or destroyed only transformed/transferred

2nd law: entropy of a system and its surroundings is is always increasing

Gibbs free energy equation

🔺G = 🔺H - T🔺S

calculating 🔺G

🔺G = G final - G initial

how do you remove the inorganic phosphate to use it for metabolic processes from an ATP?

hydrolysis

what is the initial energy investment required to start a reaction

activation energy

what is the highest energy point in a reaction

transition state

what happens when you bring an enzyme and a substrate togeher?

lowers the activation energy of a reaction

what are ways to lower EA even more than just substrate and enzyme interaction?

induced fit: enzyme will change its shape to fit the substrate better making it more reactive

environment that promotes the reaction

what happens in the enzyme active site when a substrate binds?

the side chain of the amino acid interact with the side chain of the substrate

when would a reaction rate plateau with enzymes?

when there are limited amount of enzymes and more substrates

• can increase again if you add more enzymes for the substrates to bind to

what is more efficient, irreversible inhibition or reversible inhibition

reversible because you can use the enzyme again after the substrates leave

what are factors that impact an enzymes activity

temperature, pH, cofactors

how does a product double as an inhibitor

when there is too much of it, it will be left over and bind to the enzyme stopping it from making more until needed

competitive vs noncompetitive inhibition

comp: inhibitor must compete with substrate for the active site

non-comp: inhibitor binds to the enzymes allosteric site and changes its conformation of the active site not allowing the substrate to bind

allosteric activation vs inhibition

activation: when regulatory molecule binds it increases the affinity between active site and substrate

inhibition: when regulator molecule binds it decreases the affinity between active site and substrate

what are cofactors used for"?

can be inorganic (Zn, Mg, Fe) or organic (NADH, FADH2)

• helps the enzyme function in things like unfavorable environments

NLS vs NES

short amino acid sequence that directs a protein either in (NLS) or out (NES) of the nucleus

Nuclear pore complexes

acts like a barrier only allowing certain things from the cytoplasm in the nucleus and vice versa