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Department
Biology
Course
BIOL 2020
Professor
K Wheaton
Semester
Fall

Description
Describe primary, secondary, tertiary, and AA sequence, 3D structure from the N-H &C-H quaternary structures bonds, R groups bonding (intramolecular), more than one polypeptide chain(inter and intra) small are oligopeptides or peptides Knowing the primary sequence of AA’s are 3D structure is determined by it, eludicating good because (4) its mechanism, medical reasons (point mutations or misfolds e.g. cystic fibrosis or sickle cell), knowing evolutionary history To know about ends of a polypeptide, and Amino end (beginning) and carboxyl end have peptide bond is? Which is beginning and end? different charges, and peptide bond has partial double bonding Polypeptide backbone is rich in, is a good what Hydrocarbons, hydrogen bond acceptor and and can interact with? can interact with each other and functional groups from side chains Most proteins are __ to __ in size 50-2000 AA in size Largest protein? Titin, 27,000 AA and is a contractile muscle scaffold. Molecular weight of a residue? 110 g/mol or 110 daltons Describe disulphide bridges Oxidation of a pair of cysteine residues called a cystine can be same chain or different, just in close proximity Describe the use of gel electrophoresis, type Movement depends on electric field strength, of gel, and how the proteins are separated polyacrylamide gel, movement depends on pH and shape of protein, big ones won’t move as fast and far as smaller ones Describe how SDS is used in electrophoresis It is used to charge the proteins and to denature them, it binds at a ratio of 1 for every 2 AA’s present, and that is how they are electrically charged and then a reducing agent is added to linearize the proteins. Compare to proteins of a known size to determine identity. Describe how western blot is used and can Take the SDS proteins and put them on a detect? nitro-cellulose membrane, then use specific antibodies that bind to the proteins at detect which protein it is, use a secondary antibody that will help through the detection of light, shown by phototograhpic film. Able to detect higher molecular weight forms. What is known about peptide chains 1. It is planer (one bond between 2 flexibility? (4) residues has 6 atoms On 4 , what type of bonds mostly? 2. The partial double bond from the resonance structure conforms it to be planar 3. The double bond character is expressed from the length of the bonds which is between single and double 4. Peptide bond is uncharged so that it can compact to form globular structures. Mostly trans bonds Trans and cis conformations, describe and Trans: alpha carbons are on opposite sides, which one is favored? cis: same sides, trans is favored because of steric clashes in the cis conformation Describe phi (o and stick) and psi(water thing) Phi=angle of rotation between nitrogen and torsion angles alpha carbon, psi=angle of rotation between alpha carbon and carbonyl atom ...these
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