BCH 4054 Lecture Notes - Lecture 27: Catalytic Triad, Diffraction, Globular Protein
Document Summary
Exam 3 will be on exam 8, 9 and 10. The speciicity for trypsin of one substrate comes from the negaively charged pocket. Mutaion to cys, his, asp or cys, his and glu would result in the greatest decrease in funcion of the catalyic triad. Myoglobin and hemoglobin are similar in the teriary structure. Collagen requires every third amino acid to be a glycine and is essenial to the triplet helix. The general funcion of molecular chaperones is prevening premature folding by binding hydrophobic regions of the protein. Folding a disordered polypepide into a stable protein irst aggregates the hydrophobic regions in the protein. Crystalline proteins, many crystalline protein enzyme remain catalyically acive and the difracive patern observed during x-ray exposure to the crystal can be used to calculate the electron density map of the crystalline protein. A hydropathy index can predict if an amino acid side chain will fold towards inside or outside of a globular protein.
