MCDB428Lect03 - MCDB 428 Lecture 3: Wednesday January 9,...

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Lecture 3: Wednesday January 9, 2008 Today’s Outline Protein Primary Structure Peptide bonds Polypeptide sequence Amino Acid characteristics Protein Secondary Structure Alpha helix Beta sheet, beta turn Protein Tertiary Structure Structural motifs Structural and Functional Domains Modular Organization Experimental strategies Protein Folding Protein Turnover MCDB 428
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Proteins Made of Amino Acids Joined by Peptide Bonds 20 Amino Acids distinguished by distinct R groups Average MW of an amino acid is ~110 Daltons 1 Dalton = 1 gram/mole
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Protein Polypeptides peptide bonds are planar due to resonance of double bond between C=O and C=N rotation of the polypeptide chain therefore occurs primarily between C α -C and N-C α bonds
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Characteristics of Various Amino Acids is Determined by Their Side-chains the side chains of the proteins are largely hydrophobic and therefore tend to coalesce to the inside of folded proteins One exception is Tyrosine, containing a hydroxyl group on its benzyl ring, this is capable of being phosphorylated during signaling (e.g. Tyrosine Receptor Kinases)
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Typically exposed to water Amino Acids with similarly charged side-groups tend to repel one another Salt Bridges can form between positively and negatively charged amino acids Can serve as a ubiquitin attachment site
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Amino Acids that Can Be Phosphorylated or Glycosylated Ser and Thr can be phosphorylated and are substrates for O-linked glycosylation in the Golgi lumen Asn residues are substrates for N- linked glycosylation in the ER
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Special Amino Acids Cys is capable of forming intra- or intermolecular disulfide bonds
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This note was uploaded on 09/03/2009 for the course MCDB 428 taught by Professor Wang during the Winter '08 term at University of Michigan.

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MCDB428Lect03 - MCDB 428 Lecture 3: Wednesday January 9,...

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