Met or M Phenylalanine Phe or F Tryptophan Trp or W Proline Pro or P What makes

Met or m phenylalanine phe or f tryptophan trp or w

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(Met or M) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P) What makes all Amino Acids different?
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Fig. 5-17b Polar Asparagine (Asn or N) Glutamine (Gln or Q) Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y)
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Fig. 5-17c Acidic Arginine (Arg or R) Histidine (His or H) Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Basic Electrically charged
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Peptide bond Fig. 5-18 Amino end (N-terminus) Peptide bond Side chains Backbone Carboxyl end (C-terminus) (a) (b) Polypeptide Formation
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Structure Groove Groove
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Levels of Structure The primary structure Unique sequence of amino acids Secondary structure Found in most proteins, consists of coils and folds in the polypeptide chain due to Hydrogen Bonding Tertiary structure Determined by interactions among various side chains (R groups) Fully Folded Quaternary structure Results when a protein consists of multiple polypeptide chains
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Amino acid subunits + H 3 N Amino end 25 20 15 10 5 1 Primary Structure Primary Primary structure, the sequence of amino acids in a protein, is like the order of letters in a long word Primary structure is determined by inherited genetic information
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Fig. 5-21c Secondary Structure Beta pleated sheet Examples of amino acid subunits alpha helix The coils and folds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone Typical secondary structures are a coil called an helix and a folded structure called a pleated sheet
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Fig. 5-21f
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