2023-09-21T04:10:39+03:00[Europe/Moscow] en true peptide bond, what do the polypeptides that all organisms use have in common? (hint: same buildiing blocks ), what happens in ribosomes, what substance tells ribosomes what polypeptide to make, what is the primary structure for protein (1st stage of synthesis), what is the process of DNA telling informtaion to RNA called? (DNA _____ the instructions to RNA), what is the verb for RNA sending the instructions to the ribosome, what is the genetic code?, what are some examples of properties that amino acids can have, what do properties of amino acids/polypeptides affect?, whats the alpha helix, how does the secondary structure happen (how is it bonded), whats the beta pleated sheet, what is tertiary structure primarily dependent on?, whats a disulfide bridge, what are ionic bonds (in proteins), where do hydrophobic chains go in a protein relative to the other ones, how do we know if something is a quaternary structure, whats a conjugated protein, whats a example of conjugated protein, shape of fibrous and globular protein, what function do fibrous and globular proteins have, is fibrous proteins soluble or insoluble (generally ), is globular soluble or insoluble, what is a trait of the amino acid sequence of a fibrous protein, what is a trait of the amino acid sequence of a globular protein, is fibrous or globular more stable (sensitivity to heat, pH, etc.), provide a few examples of fibrous proteins (dont need all, just a few), provide a few examples of globular proteins (dont need all, just a few), what is a difference in where the R groups are between fibrous and globular proteins? (hint: it has to do w water), what have biotechnologically produced (made by humans) proteins allowed us to do?, what are GMOs often used to do (in relation to proteins), how do proteins help with cell adhesion?, what are membrane transport proteins used for?, which category of macromolecules (carbs, lipids, etc.) are receptors (for hormones and stuff) made up of?, what are histones?, what are immunoglobins, whats rubisco, where is rubisco found in high concentrations, what type of cell in which part of the body is insulin secreted from, what does insulin do, what happened to the insulin of type 1 diabetics, whats an antigen binding site, whats rhodopsin, what is collagen, how much of the protein of the body is collagen (fraction), what does collagen do (purpose), what does the molecular structure of spider silk look like, defintion of proteome?, definitoin of genome?, what does genome determine, other than genome, what affects proteome?, how can we analyze a proteome, what is denaturation, is denaturation reversible?, what are some things that can cause denaturation, what are thermophiles flashcards

ib biology 2.4 proteins

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  • peptide bond
    c-n. c of carboxyl and n of nh2
  • what do the polypeptides that all organisms use have in common? (hint: same buildiing blocks )
    they are all made up of a combo of the same 20 amino acids. what differs is the combination
  • what happens in ribosomes
    polypeptide synthesis
  • what substance tells ribosomes what polypeptide to make
    messenger RNA (mRNA)
  • what is the primary structure for protein (1st stage of synthesis)
    amino acid sequence. its the order formed by covalent peptide bonds
  • what is the process of DNA telling informtaion to RNA called? (DNA _____ the instructions to RNA)
    transcription
  • what is the verb for RNA sending the instructions to the ribosome
    translation
  • what is the genetic code?
    sequence of bases on mRNA it tells the ribosome which amino acids to use in polypeptide synthesis
  • what are some examples of properties that amino acids can have
    polar/hydrophilic, nonpolar/hydrophobic, +/- charge (ionic )some have sulfur
  • what do properties of amino acids/polypeptides affect?
    how it folds up into a protein during the third stage
  • whats the alpha helix
    a coiled secondary protein structure. results from a hydrogen bond every fourth amino acid
  • how does the secondary structure happen (how is it bonded)
    hydrogen bonds between the H in NH3 and O in carboxyl
  • whats the beta pleated sheet
    a secondary structure of protein. formed by hydrogen bonds between parallel proteins
  • what is tertiary structure primarily dependent on?
    interactions between R groups
  • whats a disulfide bridge
    tertiary structure. strong covalent bonds between 2 sulfur atoms (from a R group) ex is cysteine
  • what are ionic bonds (in proteins)
    bond bw positively and negatively charged side chains
  • where do hydrophobic chains go in a protein relative to the other ones
    inside, because it wants to get away from the water.
  • how do we know if something is a quaternary structure
    made up of multiple polypeptide chains. the structure is dependent on interactions bw the seperate polypeptide chains
  • whats a conjugated protein
    it functions with chemical groups that aren't polypeptides quaternary structures only
  • whats a example of conjugated protein
    hemoglobin each polypeptide chain contains an iron containing molecule called a heme group.
  • shape of fibrous and globular protein
    fibrous: long and narrow. globular: spherical and rounded (globe = earth = round)
  • what function do fibrous and globular proteins have
    fibrous: structural. strength and support globular: catalyctic, transport
  • is fibrous proteins soluble or insoluble (generally )
    insoluble globular is the opposite: soluble
  • is globular soluble or insoluble
    soluble. globular = circular = water (like a water droplet) fibrous is the opposite: insoluble
  • what is a trait of the amino acid sequence of a fibrous protein
    its repetitive
  • what is a trait of the amino acid sequence of a globular protein
    the sequence is irregular. no pattern
  • is fibrous or globular more stable (sensitivity to heat, pH, etc.)
    fibrous is more stable: less sensitive, more resistant to change
  • provide a few examples of fibrous proteins (dont need all, just a few)
    collagen, myosin, actin, keratin, elastin
  • provide a few examples of globular proteins (dont need all, just a few)
    catalase, haemoglobin, insulin, immunoglobin
  • what is a difference in where the R groups are between fibrous and globular proteins? (hint: it has to do w water)
    ●●In globular proteins the hydrophobic R groups are folded into the core of the molecule, away from the surrounding water molecules, this makes them soluble. In fibrous proteins the hydrophobic R groups are exposed and therefore the molecule is insoluble.
  • what have biotechnologically produced (made by humans) proteins allowed us to do?
    •enzymes for removing stains in clothing detergent •monoclonal antibodies for pregnancy tests •insulin for treating diabetics Disease treatments
  • what are GMOs often used to do (in relation to proteins)
    they are used to produce proteins. its a difficult and expensive process though
  • how do proteins help with cell adhesion?
    they make adjacent animal cells stick together. ex: adherens
  • what are membrane transport proteins used for?
    facilitated diffusion and active transport, and also for electron transport during cell respiration and photosynthesis. diffusion = spreading
  • which category of macromolecules (carbs, lipids, etc.) are receptors (for hormones and stuff) made up of?
    proteins.
  • what are histones?
    a type of protein Histones are associated with DNA in eukaryotes and help chromosomes to condense during mitosis. it condenses/packs the dna
  • what are immunoglobins
    antibodies. a type of protein
  • whats rubisco
    ribulose bisphosphate carboxylase it is an enzyme that catylzes the reaction that turns carbon dioxide into more useful stuff (like carbohydrates), (what it turns into is kinda complicated and prob doesnt matter so prob dw about specifics)
  • where is rubisco found in high concentrations
    leaves, algal cells (in algae )
  • what type of cell in which part of the body is insulin secreted from
    beta cells in the pancreas
  • what does insulin do
    signal cells to open up to take in glucose. it therefore reduces concentration of glucose in blood (cus the glucose goes out of the blood, into the cell(s))
  • what happened to the insulin of type 1 diabetics
    they dont make enough so they need to inject some synthetic insulin
  • whats an antigen binding site
    receptor that detects molecules on a pathogen(germ) to trigger an immune response
  • whats rhodopsin
    a pigment that absorbs light . retinal molecule absorbs a single photon of light -> changes shape -> change to the opsin -> the rod cell sends a nerve impulse to the brain. it is made from opsin (polypeptide) that surrounds a prosthetic group
  • what is collagen
    rope-like proteins made of three polypeptides wound together and it strengthens stuff
  • how much of the protein of the body is collagen (fraction)
    1/4th
  • what does collagen do (purpose)
    strengthens skin + blood vessel walls (makes it resistant to tearing). prevents cracks and fractures in bones and teeth
  • what does the molecular structure of spider silk look like
    bottom has parrallel arrays and middle is more disordered
  • defintion of proteome?
    all protein produced by cell/tissue/organism
  • definitoin of genome?
    all genes produced by cell/tissue/organism
  • what does genome determine
    what proteins its possible for a organism to produce
  • other than genome, what affects proteome?
    environment
  • how can we analyze a proteome
    mixtures of proteins are extracted from a sample and are then separated by gel electrophoresis.
  • what is denaturation
    disruption or breaking of bonds between proteins (especially weak ones like hydrogen bonds)
  • is denaturation reversible?
    not usually
  • what are some things that can cause denaturation
    extreme pH and heat
  • what are thermophiles
    organisms (often archaea or eubacteria that live in relatively hot conditions (45 to122 °C). their proteins are stable at temperatures that are higher than normal.