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unit 3: proteins

BIOL 288

QuestionAnswer
what are proteins a folded (or complex of folded) polymers of amino acids
what are the functions of proteins enzymes, cytoskeletal and ECM elements, hormones, growth factors, transcriptional regulators, membrane receptors and transporters, sensors, intra and extracell transporters, contractile elements and molecular motors, molecular weaponry, nanowires, clots
how proteins enzymes catalyze metabolic/biochemical reactions. eg amylase in beer production
what is the flowchart of amylase in beer starch-glucose-glycolysis-alcohol
how proteins cytoskeletal and ECM elements provide structural and mechanical support, cell shape movement of cells and molecules
what are the types of cytoskeletal proteins actin, microtubules and intermediate filaments
how proteins hormones, growth factors, transcriptional regulators modulate a wide variety of cellular and regulatory processes
how proteins membrane receptors and transporters determine what a cell responds to and what can enter and exit
how proteins sensors detect/sense light, heat, chemicals
what are proteins intra and extracellular transporters eg. hemoglobin (transport oxygen) and rhodopsin(sense light)
hwo proteins contractile elements and molecular motors machinery for biological movement. muscle, flagella, pack DNA into virus. Bacteriophage 29 DNA packaging motor(60piconewtons)
how proteins molecular weaponry antibodies, toxin elimination, antimicrobial peptides
how proteins nanowires conductance bacterial cell pili catch with cytochomes
proteins are amino acid polymers
how many stereoisomers in amino acids 2, D and L
what are enantiomers pair of molecules that are mirror images of eachother(all but glycine)
dermorphine makes opiod on frog skin
what are the 4 groups of amino acids polar charged(hydrophilic), polar uncharged(hydrophilic), nonpolar and unique
what are the polar charged aspartic acid, glutamic acid, lysine, arginine, and histidine
what is the pka of bases and acids bases low, acids high
what are the polar uncharged serine, threonine, glutamine, asparagine, and tyrosine
which AA have amide side chain resonace glutamine and asparagine
what are nonpolar alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryoptophan
what are unique glycine, cysteine and proline
what is the insulin stuff prohormone has intra (within same molecule).C-peptide made of A and B chains. A chain has one intra disulfide bond. B chain linked to A by 2 inter disulfide bonds
what are the 21 and 22nd AA formed by stop codons. rare and specialized functions
what are posttranslationally modified amino acids occur after amino acid incorportation into the polypeptide strand
what is the function posttranslationally modified amino acids targetting/recognition of proteins, halflife/activity, interactions with other molecules, signal tranduction
what are the examples of posttranslationally modified amino acids phosphorylation, glycosylation, methylation, actelyation, sulfation and iodination
what is the primary structure of protiens linear amino acid sequence of polypeptide chain
what is the secondary structure of proteins H bonding between atoms of peptide bonds, fold in repeating and predictable patterns. local, not global. close, repetitive involves H bonds between peptide bond atoms is predictable!
what is the tertiary structure pf protiens 3D, global folding pattern driven by interactions beween amino acid side chains of the polypeptide. R group interaction, homology modeling
what is the quaternary structure of proteins 3D structure of a proteins consisting of 2 or more polypeptide chains
what is the quinary structure of proteins non-covalent interaction between molecules that organize the cellular interior. structural elements of the cell. substrate channelling
how primary structure created (in what fashion) stepwise addition of chain via dehydration, needs info and energy is activated
the peptide bond is an amide bond and has partial charge characteristics.. resonance phi and psi
the alpha helixx R groups on outside, 3.6 AA per turn. inter and intra H bonds, between CO and NH groups.
the b-pleated sheet only intra. antiparellel more straightH bonds, stronger. alpha carbon at peaks and troughs, R groups jut out
what are motifs secondary
what do molecular chaperones do prevent unwanted interactions in cytoplasm of cell.
what is teritary structure stabilized by molecular interactions and forces. disulfide bonds, H bonds, ionic bond, Van der Waal
what is the difference in globular and fibrous proteins globular are more common. fibrous are repeating and have tensile strength
what are dimer two identically repeating subunits
what is a metabolon a temporary stuctural-functional complex formed between sequential enzymes of a metabolic pathway.
what is example of substrate channeling electron transport chain(81 polypep, among 3 multisubunit complexes), citric acid cycle (3 enzymes-mMDH,CS, ACON)
Created by: abc273