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G. N. Ramachandran and his co-workers in Madras, India, first showed that it was convenient to plot to show the distribution of allowed values in a protein or in a family of proteins. Leucine zipper of yeast Interactions of two alpha helixes are common b-Sheets : (a) parallel, (b) antiparallel Interactions of b sheets Structure of PHL P2 protein β turns 1. Supersecondary Structures (Motifs) Common motifs Zinc-finger motif Three secondary structures (an ?-helix and 2 ?-strands with an anti-parallel arrangement) form a finger-like bundle held together by a zinc ion. It is often found in DNA- and RNA-binding proteins. 2. Domains Pyruvate Kinase Conservation of Cytochrome c structure. Structural similarity of LDH and MDH 4.5 Quaternary Structure Quaternary structure of multidomain proteins Typical domain structures of globular proteins 反平行螺旋束 珠蛋白型α—螺旋蛋白 单绕平行β桶 双绕平行β片 (马鞍形扭曲片) 上下型β桶 3. Domain structure and function Often a single domain has a particular function, such as binding small molecules or catalyzing a single reaction. In many cases, binding of small molecules and the formation of the active site of an enzyme take place at the interface between two separate domains. So in multifunctional enzymes, each catalytic activity can be associated with one of several domains found in a single polypeptide chain. Refers to the organization of subunits in a protein with multiple subunits (an “oligomer”) The subunits of an oligomeric protein may be identical or different. When they are identical, dimers and tetramers predominate. When they differ, each type often has a differnet function. 2. β strands and βsheet β-Strands - polypeptide chains that are almost fully extended β-Sheets - multiple βstrands arranged side-by-side = most common form of arrangement in proteins β-strands are not more stable. However β-sheets are stabilized by hydrogen bonds between carbonyl oxygens and amide hydrogens on adjacent β-strands. The β-strands in β-sheet can be either parallel
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