300936 Lecture 4: Functional proteins and genes 4

• School: UWS
• Department: University of Western Sydney
• Course: 300936
• Professor: anonymous

Document Summary

Functional proteins and genes covalent bonding: hydrogen bonding- fundamental force in intermolecular or intramolecular interactions. Formed between electronegative atom (h acceptor) in molecule and the hydrogen bonded to another electronegative atom in another molecule. In protein, hydrogen bonds can be formed within polar amino acid residues and peptide backbone. Ionic bonding: hydrophobic interaction- clustering of hydrophobic molecules in water called hydrophobic effect. Hydrocarbon chains, aromatic (ring structure containing double bonds) alcohol. Aldehydes- adds polarity, solubility, volatility; confers pleasant or unpleasant odour. Amines- adds polarity, solubility, hydrogen bonding; weak base. Organic phosphates- acidic, reactive, involved in energy transfer. Thiols- reactive, disulphide bonding: electronegativity- an atom or ions stability to pull electrons towards itself in a covalent bond. The most electronegative elements found towards top right corner of periodic table: an acid is a proton donor whereas a base is a proton acceptor. Acids ionize to form a proton and a base.