Lecture 1

Lecture 1 - Lecture 1: General Introduction and Chemical...

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Lecture 1: General Introduction and Chemical Foundations I 2.1- Atomic Bonds and Molecular Interactions: Covalent bond- when two atoms share one or multiple pairs of electrons (strong forces form covalent bonds) Weak, attractive forces of noncovalent interactions are also important in determining properties/functions of biomolecules (proteins, nucleic acids, carbohydrates, lipids) FOUR major noncovalent interactions: - Ionic interactions - Hydrogen bonds - Van der waals interactions - Hydrophobic effect H, O, C, N, P, S are the most abundant in biomolecules Form covalent bonds with other atoms Usual Number Of Covalent Bonds- Hydrogen: 1 , Oxygen: 2 , Sulfur: 2, 4, 6 , Nitrogen: 3 or 4 , Phosphorus: 5 , Carbon: 4 Carbon, which forms a tetrahedral structure, is often asymmetric It can be arranged in two forms, and forms two mirror images- a property called chirality These two mirror images are called optical or stereoisomers In many “polar” molecules, electrons are shared unequally electronegativity: extent of an atoms ability to attract an electron nonpolar bond: a bond between atoms that have identical or similar electronegativities one end of a polar bond has a partial positive charge δ +, the other has a partial negative charge δ - electric dipole: a positive charge separated by an equal but opposite negative charge (ex: O---H) H2O molecules are dipoles that form electrostatic, non covalent interactions with one another Covalent bonds are stronger and more stable than noncovalent bonds
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Energy required to break covalent bonds is much LARGER than the
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This note was uploaded on 12/02/2010 for the course BIOL 200 taught by Professor Bureau during the Fall '06 term at McGill.

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Lecture 1 - Lecture 1: General Introduction and Chemical...

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