Mitochondria and Chloroplasts
how does mitochondria reproduce
fission
what is the monomer that creates proteins and what direction is it always going to form
amino acids; N-->C or NCC
what are the two directions beta pleated sheets can form in
parallel and anti-parallel
what is competitive inhibition
inhibitor binds at the active site to stop ligand from binding, thus preventing enzyme from functioning
break down the word "synthase" (what does it mean?)
synth- = synthesize
-ase = enzyme
synthase = enzyme that synthesizes something
list the four components of the mitochondria
matrix
inner membrane
outer membrane
intermembrane space
proteins are all about the _____
shape!
what are the four levels of protein organization and explain them
primary - amino acid sequence
secondary - beta pleated sheets and alpha helices
tertiary - a 3d polypeptide chain
quaternary - multiple polypeptide chains
what is allosteric inhibition
inhibitor binds anywhere on the enzyme that isn't the active site to change the enzyme's shape so that the ligand can no longer bind to it, thus preventing the enzyme from functioning
what does a subunit refer to
a polypeptide chain within a quaternary protein
how are mitochondria and chloroplasts similar (give four examples)
both have their own genomes/DNA, proteins/ribosomes, and membrane; both reproduce on their own, both create energy
what kind of bond do amino acids use to link up (be specific)
peptide bonds (type of covalent bond)
what will happen if proteins fold incorrectly
protein folding disorders (alzheimer's disease, prion diseases, parkinson's disease)
what do protein kinases and protein phosphatases do
kinase: adds a phosphate (phosphorylates)
phosphatase: removes a phosphate (dephosphorylates)
what's a sympton of alzheimer's disease
loss of memory, cognitive decline, behavioral changes
how is ATP created during oxidative phosphorylation
a proton gradient turns electrons into ATP using ATP synthase
what is a protein domain
a small part of a protein that has a specific function
how do folded proteins maintain an amphipathic nature
nonpolar (hydrophobic) side chains cluster in the interior part of the protein and polar (hydrophobic) side chains arrange on the exterior part of the protein
give an example of positive and negative feedback
positive feedback: body needs more glucose --> gluconeogenesis
negative feedback: once enough amino acids are synthesized, the reaction stops so that no more are synthesized
what is important to remember about ligand-protein interactions
ligands and proteins are highly selective based on shape, charge, size, hydrophilic/hydrophobic, etc... (lock and key model)
glycolysis: glucose --> pyruvate and ATP
pyruvate --> acetyl coA
citric acid cycle: acetyl coA --> NADH and ATP
oxidative phosphorylation: NADH --> 30 ATP!
what are protein families
groups of related proteins that share common structural and functional features
what are the two things that help proteins fold
molecular chaperones and hydrogen bonding
what are three types of chemical modification / post-translational modification
phosphorylation
acetylation
methylation
ubiquitination
where are the binding sites on antibodies
two binding sites at the top of the y-shaped antibody