TY - CHAP M1 - Book, Section TI - Proteins: Determination of Primary Structure 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 Y1 - 2018 N1 - T2 - Harper's Illustrated Biochemistry, 31e AB - OBJECTIVESAfter studying this chapter, you should be able to:Cite three examples of posttranslational modifications that commonly occur during the maturation of a newly synthesized polypeptide.Name four chromatographic methods commonly employed for the isolation of proteins from biologic materials.Describe how electrophoresis in polyacrylamide gels can be used to determine the purity, subunit composition, relative mass, and isoelectric point of a protein.Describe the basis on which quadrupole and time-of-flight (TOF) spectrometers determine molecular mass.Compare the respective strengths and weaknesses of DNA cloning and mass spectrometry (MS) as tools for determining protein primary structure.Explain what is meant by “the proteome” and cite examples of its potential significance.Describe the advantages and limitations of gene chips as a tool for monitoring protein expression.Outline three strategies for resolving individual proteins and peptides from complex biologic samples to facilitate their identification by MS.Comment on the contributions of genomics, computer algorithms, and databases to the identification of the open reading frames (ORFs) that encode a given protein. SN - PB - McGraw-Hill Education CY - New York, NY Y2 - 2024/03/28 UR - accessmedicine.mhmedical.com/content.aspx?aid=1160188691 ER -