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Lecture 10/5/11

Bio200 w/Prof Mandy

QuestionAnswer
Polypeptide A chain of amino acids
1st structure (primary) Most basic level of protein structure. Sequence of amino acids.
2nd structure (secondary) Backbone interactions. Alpha helix and beta sheets
Alpha helix Each H-bond is weak, but there are lots so overall structure is stable.
Beta sheet Can be 2 or more strands. Can be multiple polypeptides.
3rd structure (tertiary) Overall folding "Ribbon diagram". Held together by interactions between R-Groups and other R-Groups or atoms of peptide backbone.
4 Types of R-Group Interactions 1) Ionic Bond 2) Hydrogen Bond 3) Hydrophobic Interaction "vander waals" 4) Disulfide bridge: only covalent interaction happens with 2 cysteines
4th structure (quaternary) Interactions between multiple polypeptides.
Denaturing of a protein (unfolding) Denatured-little or no function
Denatured factors Temperature, pH, salts (ions)
Renaturing sometimes possible
Life Equilibrium=death Life=fight against equilibrium
Anabolic rxns Building up
Catabolic rxns Breaking down
Anabolic rxns and Catabolic rxns Metabolism sum of all reactions
Gibbs Free Energy Ability to do work. Instability
Created by: c13luong
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