index card - tRNAs will bring in more amino acids to the dna - connect one by one = form chain until stop signal

the central dogma Flashcards by claire perez

this help to break into amino acids

digestive enzymes
(amylase, protease, lipase,lactase, sucrase, maltase)

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where do the amino acids enter after it has broken down by the digestive enzymes

bloodstream through the interior lining of the small intestine
and into the cells, where RNA molecules transcribed from genes guide their assembly into new proteins

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nonessential -
conditionally essential -
essential -

nonessential - 5
body can produce on its own
no need to get from diet
Alanine
Asparagine
Aspartate
Glutamate
Serine

conditionally essential - 6
body can make them but if have illness or stress (metabolic disease) body may not produce enough
Arginine
Cysteine
Glutamine
Glycine
Proline
Tyrosine

essential -6
cannot be made by the body
get from food/ diet
Phenylalanine
Histidine
Isoleucine
Leucine
Lysine
Methionine
Threonine
Tryptophan
Valine

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what is the structure of the amino acid

central carbon atom bonded
- hydrogen atom
- amino grp, NH2
- acid grp, COOH
- R group

*link via peptide bond

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a protein that consists of one or more long chains of amino acids

polypeptides

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shorter chains of amino acids

peptides

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a protein’s three-dimensional shape

conformation

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it is described the relationship between nucleic acids and proteins as a directional flow of information

called the central dogma
discovered by:
James Watson and Francis Crick
- their structure of DNA in 1953

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differences and similarities of dna and rna

index card

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The bases of an RNA sequence are complementary to those of one strand of the double helix

template strand

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it is the non template strand of the DNA double helix

coding strand

*the coding region
- contains the sequence of codons
- carries the genetic info for translation

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an enzyme that builds and RNA molecule

RNA polymerase

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dna polymerase vs rna polymerase

index card

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types of RNA (size)
- function

messenger RNA (500 - 4,500)
- encodes aa sequences

ribosomal RNA (100 - 300)
- associates w proteins = form ribosomes
- support and catalyze protein synthesis

translate RNA (75 - 80)
- transport specific aa to the ribosomes for protein synthesis

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where does the rRNA found

in the ribosomes
“cell’s protein making machine”

-catalyze formation of peptide bonds between amino acids

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ribosomes structure

large subunit (3 molecule)
- aka in eukaryotes: 60S subunits
- 5347 rna base
-47 proteins
- catalyze the formation of peptide bonds btwn aa

small subunit (1molecule)
- aka if in eukaryotes: 40S subunit (svedberg unit)
- 1869 rna base
- 32 proteins
- responsible for reading the mRNA during translation
-ensure that correct tRNA pairs with mRNA codons

*the ribosomes have 2 separate subunits in cytoplasm but they join at the site of the chain initiation

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tRNA structure

index card

tRNAs will bring in more amino acids to the dna
connect one by one = form chain until stop signal

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it is the protein that help control which gene to turn on or off

transcription factors
has a specific areas of thhe transcription factors called the binding domains

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what are the different type of domains

helix-turn-helix:
twisted spiral, followed by a bend, and then another spiral.

zinc fingers:
resemble a “finger” that grabs the DNA, and they often need zinc (a metal) to hold their shape.

leucine zippers:
look like a zipper, with leucine (an amino acid) acting like the teeth of the zipper that help the transcription factor hold onto the DNA

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steps of transcription

initiation:
rna polymerase attach to dna at the promoter
starts unwinding the DNA strand so it can read the gene
*promoter serves as the starting point

elongation:
RNA polymerase moves along the DNA strand
reading its sequence and building an RNA strand by adding complementary RNA bases (A, U, C, G

termination:
RNA polymerase reaches the terminator sequence (a “stop” signal) = stops transcription
made RNA is released, and RNA polymerase detaches from the DNA

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help RNA polymerase find where to start on the DNA

transcription factors

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flow of RNA processing

transcription:
cell makes a rough copy (pre-mRNA) of the DNA strand
copy includes everything - both the important parts (exons) and the unnecessary parts (introns)

modification:
cap” at the front end (5’ end) - like putting a protective cover on the beginning
“tail” at the back end (3’ end) made of many A’s - like adding a protective backing

splicing:
mRNA
cuts out introns
keeps exons
joins exons tgt

enzymes proofread the remaining RNA

final product:
mature mRNA
moves out the nucleus into the cytoplasm
- can be used to make proteins

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what are the 4 genetic code

the code is triplet
dna & rna uses 3-letter code called codon
the code does not overlap
code is read straight through in groups of three, without overlap
example: AUGCCCAAG is read as AUG-CCC-AAG (like reading word-by-word)

3.the code includes control
start” and “stop” signals built into the code
stop: UGA, UAA, and UAG
start: AUG

4.the code is same in all species
all living things (from bacteria to humans) use the same genetic code
different three-letter combinations can code for the same amino acid (synonymous codons)

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what is the minimum no. of bases in a codon

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how many does the genetic code cld specify 20 amino acids

64 different three-letter combinations to specify 20 amino acids

codons that termed different amino acids

nonsynonymous codons

different codon that specify the same amino acids

synonymous codons

the first amino acids in the protein chain

Met, methionine

terminating translation

ppt slide

where does translation take place

on free ribosomes in the cytoplasm associated with the endoplasmic reticulum - make and transport proteins

after protein is made, how many times does the protein fold into

one or more conformations - it folds to the right shape to function properly

it stabilize partially folded regions in their correct form, and prevent a protein from getting “stuck” in a useless intermediate form

chaperone proteins - help guide folding process, fold into correct shapes and don't get stuck in the middle of folding

what happens when a protein is folded incorrectly (misfolded)

a system called unfolded protein response kicks in slow or stops the protein synthesis while increasing the production of more chaperone proteins and other folding proteins to fix the problem.

it is when the misfolded proteins are sent out of the ER back into the cytoplasm, where they are "tagged" with yet another protein

ubiquitin - If a protein gets one ubiquitin tag, it might be able to unfold and refold correctly.

what happens to the misfolded protein bearing one ubiquitin tag: more than one ubiquitin tag:

one ubiquitin tag: straighten and refold correctly more than one ubiquitin tag: taken to another cellular machine called a proteasome whr it breaks down into peptides to amino acids = reuse

what are the two ways that the proteins misfold

mutation: change the aa sequences alters attractions and repulsions having more than one conformation: proteins fold into more than 1 shape = cant work properly cause problems

what are the type of disease when proteins misfold and cant do their jobs properly

Alzheimer disease Familial amyotrophic lateral sclerosis frontotemporal dementia Heredity ATTR amyloidosis Parkinson disease Lewy body dementia PKU Prion disease

what happens when one conformation becomes "infectious"

it converts molecules with other conformations into more copies of itself - basically cause other proteins of the same kind to fold into this harmful shape. It’s like a bad influence that makes healthy proteins change into a harmful form.

this is called the "infectious proteins"

prion disease - subgrp of protein misfolding sheep > scrapie proteinaceous infectious agents

proteins that can misfold and cause other proteins to misfold in a harmful way, leading to serious diseases.

prions

what is the first step in dna replication

unzip the dna helicase breaks the hydrogen bonds of the bases into 2 strands

it attaches the primers to single strand

primase

function of dna polymerase

can only add new nucleotides in the 5' to 3' direction

what are the fragments called in the lagging strand

okazaki fragments hence need ligase to connect those together

functions of proteins

blood clotting muscle contractions antibodies/ immunoglobulins hair/ skin/ connective tissue enzymes- important for biochemical functions

where do these process occur in the cell replication: transcription: translation:

replication: nucleus ("S" phase) transcription: nucleus translation: cytoplasm (ribosomes)

this RNA encodes amino acid sequence

mRNA

this RNA associates with proteins to form ribosomes, which structurally support and catalyze protein synthesis

rRNA

this RNA transport specific amino acids to the ribosomes for protein synthesis

tRNA

when do the large and small subunit come together

both come tgt during translation to form a complete ribosome

it is a sequence that binds a complementary mRNA codon

anticodon

what is the function of the transcription factor

binds DNA at certain sequence initiates transcription of specific site on chromosomes *essential in initiation and regulation

it provides binding site for transcription factors and rna polymerase

promoters

this is the first transcription factor and a binding protein that recognizes the TATA regions and bind to DNA

TATA binding protein

what happens after rna polymerase is attached to the promoter

rna polymerase will unwind small portion of dna

directionality in transcription: synthesis:

transcription: 3' to 5' on a dna template strand synthesis: synthesis of mRNA in a 5' to 3' direction

what are the modifications made in the pre-mRNA

addition of the 5' mRNA cap - modified guanine helps protect RNA help ribosomes recognize mRNA 3' poly A tail - abt 200 adenine stability afterwards it will undergo splicing (spliceosomes) remove the non coding regions, introns and combine coding regions, exons it will then exit out of the nucleus to find ribosomes to undergo translation

what type of energy is used in the translation process

ATP: initiation GTP: elongation termination

one example of quaternary structure of a protein

hemoglobin

this protein stabilize partially folded regions in their correct form and prevent a protein from getting stuck in a useless intermediate form

chaperone

CTFR protein

The CFTR protein is like a little gate that controls salt and water flow in our cells. This helps keep mucus thin, so it can clear out easily, especially in the lungs. Chaperone proteins are like helpers that make sure CFTR folds into the right shape so it can work properly. If CFTR doesn’t fold right, it can’t reach the cell’s surface, leading to thick mucus, which causes problems in conditions like cystic fibrosis.

the central dogma Flashcards

(61 cards)