ib bio mega review

ACT GTA CTC TAC —→ ACT ATG CTC TAC. What type of mutation is happening?

Substitution

Which term describes the whole of the genetic information of an organism?

Genome

In a natural classification, what do all members of a genus have in common?

All evolved from the same common ancestor

______ doesn’t determine the complexity of an organism

Genome size

Class

shared fundamental characteristics (REPTILIA!!!)

family

more specific characteristics shared (bears, dogs and wolves, cats and lions, etc)

genus

EVEN MORE SPECIFIC!! (like horses and donkeys)

Gene knockout—

gene targeted inactivated/removed from an organism to test on it and see what it would do without that gene.

 XX—

female

XY—

male

Structure of insulin?

Insulin is composed of two polypeptide chains stabilized by disulfide bonds.

What are some examples of non-coding DNA 

Promoters and telomeres

What is the function of DNA polymerase I in DNA replication?

It removes RNA primers and replaces them with DNA

How many bases would be present in the length of an mRNA molecule with 18 amino acids?

54

What makes amino acids different from each other?

The composition of the side chains

What is found in each band of DNA in gel electrophoresis?

DNA fragments with the same number of base pairs

What is the role of DNA polymerase during DNA replication?

Adds nucleotides to the growing strand

TAG is transcribed. What anticodcon on tRNA is used in translation?

UAG

What happens first in translation?

Small ribosomal subunit binds to mRNA

Which enzyme has a role similar to that of helicase in replication?

RNA polymerase

What has to be removed from two molecules of methionine to form a dipeptide?

Oxygen and hydrogen

What makes DNA semi-conservative?

One strand from the original DNA, and the other strand replicated made by DNA polymerase.

Step one of transcription

RNA polymerase III unzips/unwinds the DNA double helix

Step two of transcription

DNA polymerase III comes back to add codons to the exposed DNA strand using complementary base pairing

Step three of transcription

DNA is actively replicated using the DNA polymerase

Step four of transcription

DNA polymerase I checks the strand for errors

Step five of transcription

stop codon detected in polymerase

Step six of transcription

extrons leave and introns bind with RNA ligase

Step seven of transcription

strand is capped and mRNA is made.

1  importance of mRNA during polypeptide synthesis

Used for translating information from DNA that cannot be understood outside of the nucleus. 

2 importance of mRNA during polypeptide synthesis

Can easily travel/carry information from nucleus

3 importance of mRNA during polypeptide synthesis

Can easily help create peptides and proteins with ribosomial subunits

Basic protein structure

made from polypeptides + amino acids

Secondary protein structure

folding of alpha and beta peptide sheets cause formation

Tripeptide protein structure

continuous folding of sheets, creating a 3-dimensional structure

Quaternary protein structure

multiple (3+) peptides interacting together (ex. haemogloben)

A site rRNA

the entry point for the tRNA carrying the amino acid to be added to the growing polypeptide chain

P site rRNA

where the growing polypeptide chain is held. The tRNA molecule that is holding the growing chain is located here

E site rRNA

the tRNA molecules, now without their amino acids, are released from the ribosome.

Arabinose prevents binding of the substrate to the active site of _____

tyrosinase

What is a common feature of enzymes?

They all react with substrates

The ______ point of an enzyme catalyzed reaction graph is where active sites have changed shape

going down

What is a feature of enzyme inhibition

Non-competitive inhibitors are a different shape from the substrate

What explains a flat line in an substrate concentration on the rate of an enzyme-controlled reaction?

All active sites are occupied by substrate molecules

______ inhibitors share the same shape binding to the active site (which non-competitors don’t do) to block enzymes from doing their job, slowing the rate of reaction

competitive

______ don't share the same shape as the substrate bind to the allosteric site (which competitors don’t do) to shift the active site so the substrates are unable to bind and do their job, slowing the rate of reaction

Non-competitive inhibitors

Enzymes have a slower ROR in ______ temperatures, while enzymes have a higher ROR in _____ temperatures. The ROR and metabolism are at the mpst efficient point in the optimal temperature range, the highest point.

colder, warmer

______ enzymes and other molecules working inside of the cell for metabolism

Intracellular enzymes

_____ enzymes and other molecules working outside of the cell and metabolism.

Extracellular enzymes

What do enzymes have to do with activation energy?

Enzymes speed up the activation energy for metabolism and all other organisms and also allows metabolism to operate at body temperature.

What is the byproduct of metabolic reactions that endotherms use? Why?

Heat in endotherms from the need to keep the body at the right temperature to function properly and helps us break down food quickly.

_____ would be the highest on a graph where the slope is about to decrease.

Hydrolysis

Outline the reason for the decrease in the percentage of active amylase after 40 Celsius

As the temperature increased, exceeding the optimal point/temperature, the enzymes begin to denature, now unable to work and carry out tasks efficiently.

How is energy carried that is released during ETC?

As reduced NAD

Which part of aerobic respiration directly involves oxygen molecules?

Accepting electrons at the ETC

Where does acetyl CoA formation occur in the cell?

Matrix (middle)

Where are protons pumped, to allow chemiomosis in aerobic respiration to occur?

From the matrix of the mitochondrion to the space between the membranes

Which equation is an example of decarboxylization?

Pyruvate → Acetyl CoA + Co2

What molecule functions as te final electron acceptor in the mitochondrial electron transport chain?

Oxygen

What distinguishes aerobic respiration from anaerobic respiration in humans

Only aerobic respiration produces carbon dioxide

What type of reactions are isocitrate and oxalosuccinate undergoing?

Oxidization and decarboxylation

What type of reaction is occurring in the link reaction?

NAD+ is reduced

At what stages is carbon dioxide produced?

Link reaction and Krebs cycle

Ultimately, the molecule goes through ATP production to produce ATP and pyruvate. This happens twice. Creates 2 NADH, 2 ATP, and two pyruvate.

Glycolysis

produces two NADH, two Co2, and two acetyl-CoA.

Linking Reaction

They go through many reactions, turning FAD+ into FADH, NAD+ into NADH, and ADP into ATP. Ends with 6 NADH, 4 CO2, 2 FADH, and 2 ATP

Krebs Cycle

Electrons travel through the pumps, heading towards ATP synthase to power the pumps. Protons in the top go through ATP synthase, creating ATP.

ETC and chemiomiosis

is reduced NAD+, helps carry electrons and hydrogen ions (protons) to the ETC to become ATP

NADH

FADH2

does the same as NADH, but is only used once in the krebs cycle before being transported to the ETC. Provides less energy for the pumps.

aerobic respiration

in the mitochondria, uses oxygen, produced a net amount of 32 ATP

anaerobic respiration

only in cytoplasm, used when theres no oxygen, produces a net amount of 2 atp