MCELLBI C100A Lecture Notes - Lecture 3: Grb2, Tyrosine, Zap70
15 Sep 2015
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Document Summary
Amphipathic helices and strands secondary structural elements in soluble proteins are usually amphipathic. Protein structures are built up in an hierarchical fashion: motifs, domains. Domains are combined to make a rich diversity of proteins from simpler building blocks. Coiled-coil domains the coiled-coil is a very common structural motif involving helices. Coiled-coil structures, like the one shown here, can be very long (100 or longer). In contrast, very long two-stranded sheets are never seen in nature. Lecture 3 page 10 i, i+7 pattern in helices. Heptad repeats in coiled-coils coiled-coil segments have a characteristic i, i+4 sequence repeat. Proteins with several helices have arrangements that are not coiled coils. Conservation of protein folds protein structures are remarkably conserved in terms of three-dimensional structure across evolution. Helices pack with ridges on one helix fitting into grooves on the other: myoglobin_helix_packing. Active sites are located at the core elements of protein structure. Active sites are also commonly located at the interfaces between domains:
