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Life Science (261)
LIFE 210 (38)
Lecture

Amino acids, peptide bonds, protein folding and structure, Ras

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Department
Life Science
Course
LIFE 210
Professor
Paul Laybourn
Semester
Fall

Description
31 August Overview – Proteins Last step in gene expression, are final product Constitute most of the dry mass of cells Carry out most of the cellular functions Structure dictates function Protein structure and function builds directly on the concepts and principles we covered in lectures 1 – 4 Building Blocks – amino acids (a.a.) 20 common a.a. Convention for writing/drawing is N to C General a.a. structure α carbon – central C of amino acid Carboxyl group on right Amino group on left R group – differs between a.a. Positive charge on amine group end, negative charge on carboxyl group end R Group Classifications Hydrophilic – polar Charged Acidic Negative charge Form H & ionic bonds Basic Positive charge Form H & ionic bonds Uncharged Form H bonds Hydrophobic Form hydrophobic interactions & van der Waals Special Are nonpolar Proton Basically no R group Glycene Form hydrophobic interactions and van der Waals Prolene Hydrocarbon chain bends back and bonds covalently to N of amine group Forms hydrophobic interactions & van der Waals Cystines Sulfhydryl group Forms disulfide bonds – stabling structures for proteins Some polar R groups are charged at the appropriate pH Peptide bonds link amino acids – dehydration synthesis Between C of carboxyl group & N of amine group Peptide Bonds in Protein Folding Have resonance Electrons jump back and forth – C=O or C=N Partial double bond Planar structure Restricted rotation R groups and C=O groups can clash Steric Protien Folding and Structure – four levels Denatured – unfolded Native – renatured or properly folded Primary Structure (1°) “Sequence” of amino acids (N to C) Met-Ala-Ser-etc. M-A-S-etc. n 20 possible sequences, where n = # a.a. Connected by peptide bonds (covalent) Secondary Structure (2°) – initial folding
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