Chapter 3 - Chapter 3 Hydroxyl R-OH Aldehyde R-CH=O Ketone...

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Chapter 3 Hydroxyl R-OH Aldehyde R-CH=O Ketone R-C=O R’ Carboxyl R-C=O OH Sulfhyl –SH Phosophate –OPO 3 Condensation H-XXXX-OH + H-XXXX-OH H-XXXX-XXXX-OH + H 2 O Can be repeated to form polymers Hydrolysis H-XXXX-XXXX-OH +H 2 O H-XXXX-OH + HXXXX-OH Putting H 2 O back in there, breaks up polymer into monomers Proteins -Used in energy and information storage -polymer of amino acids -variety in the sequence determines structure and function H NH 3 + -C-COO - R (1-20) -central alpha carbon exhibits optical ability - Some amino acids have an ionic charge to attract dipoles and opposite charges -Some amino acids have a polar charge to attract other polar charges -Some amino acids don’t have any charge and are hydrophobic -cystine ( R is SH) can make disulphide bridges ( -S-S- (COVALENT)) which are present in tertiary structures -glycine (R is –H) doesn’t exhibit chirality and can fit into small bends and corners -proline has a ring fused to the amino nitrogen, so one less H is present; also, ring prevents much rotation about alpha carbon Peptide bonds - for a protein to form, the L-amino acids monomers must react between their amino (N- terminus side) and their carboxyl groups (C-terminus side) - is a condensation rxn NH 3 + -C-COO - + NH 3 + -C-COO - NH 3 + -C-C(O)-NH-C-COO - -Read from amino to carboxyl (N C) Levels of Protein Structure
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This note was uploaded on 09/15/2009 for the course MOLECULAR 20A taught by Professor Dalbey during the Winter '09 term at UCSC.

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Chapter 3 - Chapter 3 Hydroxyl R-OH Aldehyde R-CH=O Ketone...

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