RT Book, Section A1 Kennelly, Peter J. A1 Rodwell, Victor W. A2 Rodwell, Victor W. A2 Bender, David A. A2 Botham, Kathleen M. A2 Kennelly, Peter J. A2 Weil, P. Anthony SR Print(0) ID 1160188794 T1 Proteins: Higher Orders of Structure T2 Harper's Illustrated Biochemistry, 31e YR 2018 FD 2018 PB McGraw-Hill Education PP New York, NY SN 9781259837937 LK accessmedicine.mhmedical.com/content.aspx?aid=1160188794 RD 2024/03/28 AB OBJECTIVESAfter studying this chapter, you should be able to:Indicate the advantages and drawbacks of several approaches to classifying proteins.Explain and illustrate the primary, secondary, tertiary, and quaternary structure of proteins.Identify the major recognized types of secondary structure and explain supersecondary motifs.Describe the kind and relative strengths of the forces that stabilize each order of protein structure.Describe the information summarized by a Ramachandran plot.Summarize the basic operating principles underlying three key methods for determining protein structure: X-ray crystallography, nuclear magnetic resonance spectroscopy, and cryo-electron microscopy.Indicate the present state of knowledge concerning the stepwise process by which proteins are thought to attain their native conformation.Identify the physiologic roles in protein maturation of chaperones, protein disulfide isomerase, and peptidylproline cis–trans isomerase.Describe the principal biophysical techniques used to study tertiary and quaternary structure of proteins.Explain how genetic and nutritional disorders of collagen maturation illustrate the close linkage between protein structure and function.For the prion diseases, outline the overall events in their molecular pathology and name the life forms each affects.