Abstract
This chapter discusses the fundamental chemical structure of proteins, including protein conformation, mainchain, sidechains, and common post-translational modifications. It clarifies the differences between primary, secondary, tertiary, and quaternary structures. It clarifies the use and technique of polyacrylamide gel electrophoresis and mass spectrometry. It notes the power of experimental methods such as X-ray crystallography, nuclear magnetic resonance spectroscopy, and cryo electron microscopy for protein structure determination. The chapter looks at the principles of classifications of protein folding patterns. It notes the invisibility of numerous properties of proteins in genome sequences. It considers diseases of protein aggregation, citing the difficulties and possibilities of protein structure prediction and structural genomics projects. Finally, it considers the generation of useful artificial proteins, both by directed evolution and by a priori design.
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