page_title: Alpha helix
section_title: In art
hierarchical_section_title: Alpha helix / In art
caption_attribution_description: English: Artist: Julian Voss-Andreae Shown sculpture: "Alpha Helix for Linus Pauling" (2004), height 10' (3 m), powder-coated steel, location: 3945 SE Hawthorne Blvd, Portland, OR 97214 Photographer: Julian Voss-Andreae Photo taken Spring 2004
context_page_description: The alpha helix is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence.
  The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.6₁₃-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond.
  Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent.
context_section_description: At least five artists have made explicit reference to the α-helix in their work: Julie Newdoll in painting and Julian Voss-Andreae, Bathsheba Grossman, Byron Rubin, and Mike Tyka in sculpture.
  San Francisco area artist Julie Newdoll, who holds a degree in Microbiology with a minor in art, has specialized in paintings inspired by microscopic images and molecules since 1990. Her painting "Rise of the Alpha Helix" (2003) features human figures arranged in an α helical arrangement. According to the artist, "the flowers reflect the various types of sidechains that each amino acid holds out to the world". This same metaphor is also echoed from the scientist's side: "β sheets do not show a stiff repetitious regularity but flow in graceful, twisting curves, and even the α-helix is regular more in the manner of a flower stem, whose branching nodes show the influence of environment, developmental history, and the evolution of each part to match its own idiosyncratic function."
  Julian Voss-Andreae is a German-born sculptor with degrees in experimental physics and sculpture. Since 2001 Voss-Andreae creates "protein sculptures" based on protein structure with the α-helix being one of his preferred objects. Voss-Andreae has made α-helix sculptures from diverse materials including bamboo and whole trees. A monument Voss-Andreae created in 2004 to celebrate the memory of Linus Pauling, the discoverer of the α-helix, is fashioned from a large steel beam rearranged in the structure of the α-helix. The 10-foot-tall (3 m), bright-red sculpture stands in front of Pauling's childhood home in Portland, Oregon.
  Ribbon diagrams of α-helices are a prominent element in the laser-etched crystal sculptures of protein structures created by artist Bathsheba Grossman, such as those of insulin, hemoglobin, and DNA polymerase. Byron Rubin is a former protein crystallographer now professional sculptor in metal of proteins, nucleic acids, and drug molecules –  many of which featuring α-helices, such as subtilisin, human growth hormone, and phospholipase A2.
  Mike Tyka is a computational biochemist at the University of Washington working with David Baker. Tyka has been making sculptures of protein molecules since 2010 from copper and steel, including ubiquitin and a potassium channel tetramer.
caption: Julian Voss-Andreae's Alpha Helix for Linus Pauling (2004), powder coated steel, height 10 ft (3 m). The sculpture stands in front of Pauling's childhood home on 3945 SE Hawthorne Boulevard in Portland, Oregon, USA.
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