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  The structural diversity of natural coiled coils

Lupas, A., Dunin-Horkawicz, S., Martinez-Goikoetxea, M., Hartmann, M., & Hernandez Alvarez, B. (2022). The structural diversity of natural coiled coils. In 8th Alpbach Workshop: Coiled Coil, Fibrous and Repeat Proteins (pp. 39).

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Genre: Meeting Abstract

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 Urheber:
Lupas, AN1, Autor                 
Dunin-Horkawicz, S1, 2, Autor                 
Martinez-Goikoetxea, M1, Autor                 
Hartmann, M1, 3, Autor                 
Hernandez Alvarez, B1, 4, Autor                 
Affiliations:
1Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society, ou_3371683              
2Structural Bioinformatics Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society, ou_3606657              
3Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477392              
4Conservation of Protein Structure and Function Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society, ou_3477388              

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 Zusammenfassung: Seventy years ago, Francis Crick introduced the coiled coil to account for the structural

properties of proteins referred to as ‘k-m-e-f’, for keratin, myosin, epidermin, and fibrinogen. His model envisaged 2 or 3 α-helices wound around each other in parallel orientation, systematically interlocking their side chains along the fiber in a pattern that would repeat every seven residues (the heptad repeat), specifying a supercoil of opposite handedness to that of the α-helix. Since then, the coiled-coil fold has been found to be vastly more diverse, encompassing structures of between two and more than 20 helices in parallel or antiparallel orientation, which may form fibers, levers, tubes, funnels, sheets, spirals, and rings. It covers periodicities leading to both left-handed and right-handed supercoils (and to straight helical bundles in between); and includes local departures from α-helical structure such as 310 -helices, π-turns, and even short β-strands, as in the α/β-coiled coils. Here we will describe how a few simple biophysical rules can produce such a seemingly endless diversity.

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 Datum: 2022-09
 Publikationsstatus: Online veröffentlicht
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Veranstaltung

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Titel: 8th Alpbach Workshop: Coiled Coil, Fibrous and Repeat Proteins
Veranstaltungsort: Alpbach, Austria
Start-/Enddatum: 2022-09-04 - 2022-09-09

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Titel: 8th Alpbach Workshop: Coiled Coil, Fibrous and Repeat Proteins
Genre der Quelle: Konferenzband
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Seiten: - Band / Heft: - Artikelnummer: - Start- / Endseite: 39 Identifikator: -