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Home > Art, Film & Photography > Protein Structural Motifs: Alpha Helix, Beta Sheet, Collagen Helix, Transmembrane Domain, Zinc Finger, Ef Hand, Coiled Coil, Ankyrin Repeat
Protein Structural Motifs: Alpha Helix, Beta Sheet, Collagen Helix, Transmembrane Domain, Zinc Finger, Ef Hand, Coiled Coil, Ankyrin Repeat

Protein Structural Motifs: Alpha Helix, Beta Sheet, Collagen Helix, Transmembrane Domain, Zinc Finger, Ef Hand, Coiled Coil, Ankyrin Repeat


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About the Book

Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Pages: 36. Chapters: Alpha helix, Beta sheet, Collagen helix, Transmembrane domain, Zinc finger, EF hand, Coiled coil, Ankyrin repeat, RING finger domain, Alpha sheet, Basic-helix-loop-helix, Turn, Pentapeptide repeat, Short linear motif, Walker motifs, Leucine-rich repeat, Aldo-keto reductase, Polyproline helix, PHD finger, Beta helix, Granin, Kelch motif, Sterile alpha motif, Pi helix, Structural motif, Protein I-sites, Leucine zipper, F-box protein, Inhibitor of apoptosis domain, Helix-turn-helix, 310 helix, Beta bulge, Autochaperone, Rossmann fold, Beta hairpin, Knobs into holes packing, Supersecondary structure, Heptad repeat, Omega loop, Greek key. Excerpt: A common motif in the secondary structure of proteins, the alpha helix ( -helix) is a right-handed coiled or spiral conformation, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier ( hydrogen bonding). This secondary structure is also sometimes called a classic Pauling-Corey-Branson alpha helix (see below). Among types of local structure in proteins, the -helix is the most regular and the most predictable from sequence, as well as the most prevalent. In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of 5.1 angstroms (0.51 nm). Astbury initially proposed a kinked-chain structure for the fibers. He later joined other researchers (notably the American chemist Maurice Huggins) in proposing that: Although incorrect in their details, Astbury's models of these forms were correct in essence and correspond to modern elements of secondary structure, the -helix and the -strand (Astbury's nomenc...


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Product Details
  • ISBN-13: 9781155256467
  • Publisher: Books LLC, Wiki Series
  • Publisher Imprint: Books LLC, Wiki Series
  • Height: 246 mm
  • No of Pages: 38
  • Spine Width: 2 mm
  • Weight: 86 gr
  • ISBN-10: 1155256468
  • Publisher Date: 23 Aug 2011
  • Binding: Paperback
  • Language: English
  • Returnable: N
  • Sub Title: Alpha Helix, Beta Sheet, Collagen Helix, Transmembrane Domain, Zinc Finger, Ef Hand, Coiled Coil, Ankyrin Repeat
  • Width: 189 mm


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