BIO130H1 Lecture Notes - Lecture 2: Van Der Waals Force, Disulfide, Alpha Helix
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BIO130H1 Full Course Notes
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Document Summary
Electrostatic attractions: ionic bonds, very strong in absence of water. Hydrogen bonds: polar interaction, strongest when in straight line. Van der waal forces: dipole, flickers, constantly moving, clouds of e-, not weakened by h2o, when things are stacked. Hydrophobic forces: force generated by water, pushing hydrophobic parts of molecules together. Bases forced into the center by hydrophilic, polar backbone. Nucleotides are linked by phosphodiester bonds (covalent, very strong) Strands are anti-parallel, 3" (hydroxyl group) to 5" (phosphate group) They have major and minor grooves, major grooves give space for things too attach, like dna binding proteins. Is something happens to 1, we have another strand of dna to build off of still. Protein structure: primary: aa sequence, linear, secondary (local folding): alpha helix, beta sheet, tertiary (long-range folding): 3. d structure, quaternary (multimeric organization): many polypeptide chains, ex. Hemoblobin: multiprotein complexes: molecular machines, 100s of proteins, ex.
