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unit 3: proteins
BIOL 288
| Question | Answer |
|---|---|
| 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) |
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