BCH210H1 Lecture 1: Lecture 1 Elements of Protein Structure

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Reinhart Reithmeier

Document Summary

Heme (binds the iron, which binds oxygen) prosthetic group. Prosthetic group: a non-protein group, combined with or forming a protein. Glu6val (meaning: glutamate in the 6th amino acid position- switched to valine) Valine substitution causes long polymers to form, thus changes the shape of hemoglobin. Glutamate (hydrophilic) valine (hydrophobic: changes the protein interaction changes folding & 3d structure. Proteins: polymers of amino acids linked by peptide bonds. Fold from linear amino acids to 3d structure: specificity of amino acids dictate folding, mutation in dna different amino acids changes the protein functionality *and can be inherited* Function of water: solvent and a reactant. Ionic interactions (opposite charges attracting, similar repelling: results in protein stability. Van der waals interactions: important in folding. Non-polar interiors: very little water inside the protein packed tightly like crystalline structure. Hydrophilic aa"s interact with solvent on protein surface (aka water) Ultimate source of energy = the sun. Body uses 2 forms: atp & nadph.