Bio 1002 Lecture 3 Notes

Bio 1002 Lecture 3 Notes - Bio 1002 Tom Haffie Lecture 3...

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Bio 1002 Tom Haffie Lecture 3 The PROTEIN section of the Purple Pages of the textbook - specifically from page F29 - F35. 1. Basic structure of an amino acid and what are the different classes of amino acids. o Basic Structure: carbon atom attach to 1) amino group (--NH 2 ); 2) Carboxyl Group (--COOH); 3) hydrogen atom 4) --R o Classes: 1) Nonpolar AA ; 2) Uncharged polar AA ; 3) Positively charged, polar AA ; 4) Negatively Charge, Polar AA 2. Chemistry of the peptide bond and how it is formed. o Dehydration synthesis reaction between Carboxyl Group and Amino Group o Amino acids are only added to the --COOH end of the growing peptide strand! 3. The four levels of protein structure. 4. What bonding arrangements give rise to primary, secondary and tertiary structure. o A polypeptide chain is a string of amino acids, WHILE a protein is a polypeptide chain folded into a specific 3D conformation (a 3D shape is
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Unformatted text preview: required to be functional ). The 4 levels are: 1. Primary --> Polypeptide Chain --> Sequence of amino acids --> Linear 2. Secondary --> linear strand folded based on hydrogen bonds --> bonding caused by backbone H & O interaction 3. Tertiary --> overall three dimensional folding of a polypeptide chain --> bonding caused by R groups 1. Ionic Bonds 2. Hydrogen Bonds 3. Hydrophobic (non-polar) Interactions 4. Disulfide Bridges 4. Quaternary --> two or more tertiary proteins (multiple chains) 4. How are alpha helices and beta sheets formed. o Both occur as a Secondary Protein Structures 2. Alpha Sheet --> hydrogen bonds from between every N-H and C=O bond of the back bone ( cylindrical spiraling ) 3. Beta Sheet --> 2 strands, side by side hydrogen bonding! ( flattened paper fan )...
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