Chemistry 1027A/B Lecture Notes - Triple Helix, Hydroxyproline, Equilibrium Constant
18 May 2014
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Document Summary
Protein surfaces have a huge variety of shapes and charge distribution. Due to variety of amino acid side chains and many arrangements of secondary and tertiary structure. Ligand: a molecule that can bind to a protein. Many proteins contain sites to which ligands specifically bind to form a complex w/ the protein. Binding occurs by multiple weak forces (leads to extreme specificity) Hemoglobin is a tetramer (4 individual polypeptide subunits) Kd (dissociation constant): a measure of the strength or affinity of an interaction. High affinity = tight binding = small kd. Tight binding requires the cooperative formation of many weak bonds. Kd"s in biological situations range from femtomolar (very high affinity) to millimolar (low affinity) Group of proteins that work together to perform some job within the cell. Specific complex of more than 50 protein + rnas. Each protein within the complex must recognize and bind to others in the complex, thus assembling into a.
