av Tina Do 3 år siden
158
Mer som dette
Location: Mitochondrial matrix
Input: 2 Acetyl CoA
Output: 6 NADH, 2 FADH2, 2 ATP
Net products 6 NADH, 2 FADH2, 2 ATP
Location: Cytosol, then mitochondrial matrix
Input: 2 pyruvate, 2 CoA
Output: 2 Acetyl CoA, 2 NADH
Net products: 2 Acetyl CoA, 2 NADH
Doesn't produce ATP
Location: Proteins in inner membrane
Input: Oxygen gas, 10 NADH, 2 FADH2
Output: Water, 30-32 ATP
Net products: Water, 30-32 ATP
Produces ATP through the coupling of Chemiosmosis with electron transport chain
Electron transport chain: Electron transport and pumping of protons (H+),which create an H+ gradient across the membrane.
Chemiosmosis: ATP synthesis powered by the flow of H+ back across the membrane
Hydrogen ions are pumped to intermembrane space
Location: Cytosol
Input: 1 Glucose, 2 ATP
Output: 2 pyruvate, 2 NADH, 4 ATP
Net products: 2 Pyruvate, 2 NADH, 2 ATP
Produces ATP with substrate level phosphorylation
There are 6 tyrosine amino acids and they each need a phosphate group to activate so the kinase removes...
Substrate level phosphorylation: Production of ATP or GTP through the direct addition of a phosphate group to ADP or GDP
Signal molecule binds to the kinase receptors
Dimer - when the two polypeptides that have a total of 6 tyrosine portions come together
Active tyrosine kinase region - its activated just because a dimer is formed. However it is not fully activated unless phosphate groups are attatched to the tyrosines.
Kinase - an enzyme that removes one phosphate group from ATP
ATP - Adenosine tri-phosphate. The main form of how a cell carries energy
kinase removes a phosphate group from ATP and forms...
ADP - Adenosine di-phosphate. ATP with a phosphate group removed
6 phosphate groups - the result of the kinases removing a phosphate group from each ATP
Tyrosine - an amino acid that needs a phosphate group attachment to activate
Fully activated tyrosine kinase region - when the tyrosine kinase is now able to induce a response from the cell
Now that the tyrosine kinase is fully activated inactive proteins come to it
Inactive relay proteins - proteins that relay a messages but aren't doing their job because they haven't been activated.
After interacting with the tyrosine kinases the inactive relay proteins receive a message so they become...
Active relay proteins - the relay proteins are now ready to relay a message after they've been activated.
After a long process of interacting with different relay proteins the cell can now induce a...
Cellular response - anything the signal molecule wants to the cell to do after the long events of protein interactions.
The last protein that activates brings the response form the cell.
binds to an enzyme
changes shape and activates
cellular response
protein-protein interaction help position the initiation complex on the promoter
the repressor/activator interacts with the RNA poly II to help reduce/increase transcription rates.
activator/repressor elements come the last activated molecule activated in transduction
critical for precise regulation of gene expression
distal control elements
enhancers
sequences upstream and downstream of gene
maybe close or far from the gene they control
bin specific transcription factors (activators/repressors)
proximal control elements
sequences closer to the promoter
bind general transcription factors
like activators and repressors, they bind to distal control elements called enhancers
bring about increase levels of transcriptions (activators)
bring low levels of transcription (repressors)
enhancer sequences can be present close to the gene they control or on the other side.
bind to the promoters and regions near the promoter to bring about basal or background level of transcription
This will block the attachment of RNA polymerase to the promotor.
This shuts down transcription
DNA bending proteins come and bring the activators closer to the promoter
The activators bind to mediator proteins and general transcription factors
an active transcription initiation complex is formed on the promoter
A chain reaction of secondary messengers occurs
The last signal molecule serves as a activator or a repressor in a transcription factor
The Ribosome making the protein is bound to a signal recognition particle
The ribosome SRP complex is now bound to the rough endoplasmic reticulum.
The SRP leaves and the ribosome continues with protein synthesis.
The signal enzyme is cleaved by an enzyme in the rough ER which causes the ribosome to break apart leaving the protein alone.
The protein is then folded into its final shape
The protein is then moved into the Golgi apparatus
From the Golgi apparatus the protein is packaged and shipped to wherever it's needed in the body
The proteins are made useful in Eukaryotic cells with organelles such as mitochondria, Chloroplast, peroxisomes, and the nucleus
The trna with the correct anti codon matches with the codons in mrna in the ribosome
The ribosome uses its EPA site to guide the trna and its proteins until a release factor stops the process
The stacked up amino acids from trna forms a protein
Ribosome
Polypeptide chain separates from tRNA
Chain gets released
Initiation
Recognition of the start codon (5'AUG)
Binding of ribosome subunits
Elongation
P- site & A- site
P- peptide chain
DNA template
+1 Transcription start point
INITIATION
addition of transcription factors (proteins)
RNA polymerase
RNA polymerase II
RNA polymerizes bind to the promoter and make a new strand of mRNA in the 5' to 3' direction.
ELONGATION
the RNA polymerase moves downstream adding RNA nucleotides elongating the RNA transcript in the 5' to 3' direction.
TERMINATION
RNA transcript is released and the polymerase is released form the DNA
5'cap & 3'polyA sequences
Exons & Introns
introns help to alternate spacing
RNA Processing
introns are removed to bind exons
introns are released by RNA complex and Spliceosome protein.
Organelle movement
Protein Kinesin
Vesicle
Grow in centromes and pair in centrioles
Help chromosome movement
Cilia & Flagella
Nuclear lamina
Keratin Family
Plant Cells
Central Vacuole
Use to move nutrients
Provide Support
Muscle contraction
Myosin & Actin Protein interaction
ATP
Amoebiod movement
two types of regulation
negative regulation
repressor- regulatory protein
methionine(MetJ)
positive regulation
activator- regulatory protein
CAP protein
Archaea
Bacteria
Structures
Cell wall: Maintains cell shape, protects the interior of the cell, and prevents bursting of the cell after taking up water.
Contains peptioglycan
Plasma membrane
Surrounds the cytoplasm , separating it from the environment outside.
Ribosomes
Protein sythesis
Nucleoid: Holds cells DNA.
Includes Proteins and enzymes that transcribe DNA & RNA that also aid in cell growth .
glycerol
hydrophilic fatty acid head
hydrophobic fatty acid tails
saturated
fluid and not tightly packed (good)
unsaturated
viscious and tightly packed (bad)
regulates movement of phospholipids
G protein coupled receptor
signal molecule
G protein coupled receptor (GPCR)
GPCR becomes activated
Tyrosine Kinase Receptor
molecule comes from another cell
