BIO130H1 Chapter Notes - Chapter 2.8-2.12: Nuclear Magnetic Resonance, X-Ray Crystallography, Globular Protein

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BIO130H1 Full Course Notes
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Some proteins change due to posttranslational modifications (ptms) Primary, secondary, tertiary, and quaternary structures of proteins. Secondary structures: the conformations or 3d shape: alpha helix backbone non-polar residues in middle, side chains and polar residues out. Stabilized by h-bonds between peptide bonds above and below each one (o and n-h: beta sheet hydrogen bonds connect 2 chains of aa parallel or antiparallel each other; very strong and stable (silk) Stabilized by noncovalent bonds between side chains in the protein: x-ray crystallography (protein has to be large but provide high res images) or nuclear magnetic. Resonance (nmr has to be smaller but is fast) is used to determine structure. Fibrous proteins: long shape to resist pulling; mainly found outside cells and are structural materials: globular proteins: compact shape; mostly found within the cells, disorderged segments exist, which usually have charged and polar residues and little hydrophobic residues.

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