Transcription of PROTEINS: THREE-DIMENSIONAL STRUCTURE
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PROTEINS: THREE-DIMENSIONAL STRUCTURE
CHAPTER 6 PROTEINS: three -DIMENSIONALSTRUCTURE1. secondary STRUCTUREA. The Peptide GroupB. Regular secondary STRUCTURE : The aHelix and thebSheetC. Fibrous ProteinsD. Nonrepetitive protein Structure2. tertiary STRUCTUREA. Determining protein StructureB. Motifs (Supersecondary Structures) and DomainsC. protein Families3. quaternary STRUCTURE AND SYMMETRY4. protein FOLDING AND STABILITYA. Forces That Stabilize protein StructureB. protein Denaturation and RenaturationC. protein Folding PathwaysD. protein Dynamics124 The atomic STRUCTURE of myoglobin, an oxygen binding protein , is drawn here as a stick model. The overall conformation of aprotein such as myoglobin is a function of its amino acid sequence. How do noncovalent forces act on a polypeptide chain tostabilize its unique THREE-DIMENSIONAL arrangement of atoms? [Figure copyrighted by Irving Geis.]For many years, it was thought that proteins were colloids of random struc-ture and that the enzymatic activities of certain crystallized proteins weredue to unknown entities associated with an inert protein carrier.
A protein’s quaternary structurerefers to the spatial arrangement of its subunits. The four levels of protein structure are summarized in Fig. 6-1. Section 6-1. Secondary Structure125 Figure 6-1. Levels of protein structure. (a) Primary structure, (b) secondary structure, (c) tertiary structure, and (d) quaternary structure.
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