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ecs 129 Forewords Introduction Nucleic Acids Proteins: Amino Acids Proteins: Secondary and Tertiary Structures Lecture Notes Summary Molecular Viewer Supporting Papers Supplementary materials Quiz Sequence Comparison Protein Structure Classification RNA Structure Prediction Protein Structure Prediction Protein Protein Interaction Docking Databases Review Quick links pakoehl@ucdavis.edu

Patrice Koehl's teaching web site > ecs 129 > Proteins: Secondary and Tertiary Structures > Summary Personal tools Log in Summary Proteins: Secondary and Tertiary Structures There are 3 major types of secondary structures: alpha-helices, beta-sheets and beta-turns Most helices in proteins are alpha-helices, statibilized through a network of CO(i) --- HN(i+4) hydrogen bonds. Beta-strands pair to form beta-sheets. There are two types of beta-sheets: parallel, and anti-parallel Beta-turns correspond to 180 degree change in the backbone direction There are three main classes of proteins: all Alpha, all Beta, and Alpha+Beta. The latter can be divided into two sub-classes, considering the proteins with alternating alpha/beta as defining their own class The most common all-Alpha proteins are bundles (3, or 4 helices) Common all Beta proteins include greek keys, jellyrolls and sandwiches. More unusual beta structures include the beta propeller and the beta helix. The Rossman fold (alternating alpha/beta) is a very common motif in proteins. It is found in the alpha/beta barrel, in the doubly wound topology, and in the "horseshoe" geometry

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