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Radiation Safety Problems in the Caspian Region pp 57–67Cite as

Structure of Met30-Ser40 Segment in N-Terminus of Human Tyrosine Hydroxylase Type1

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Part of the book series: Nato Science Series: IV: Earth and Environmental Sciences ((NAIV,volume 41))

Abstract

Theoretical conformational analysis was performed to stretch of Met30-Ser40 amino acid residues from the N-terminus of human tyrosine hydroxylase type 1(hTH1). Eight types of stable conformations of the sequence with significantly different values of dihedral angles are possible. Two β-turns of the polypeptide chain in an aqueous environment were revealed on the section Pro32-Ile35 and Phe34-Arg37.

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Authors and Affiliations

  1. Baku State University, Z. Khalilov, 23, AZ 1043/1, Baku, Azerbaijan

    Irada N. Alieva, Narmina Mustafayeva & Dshavanchir Aliev

Authors
  1. Irada N. Alieva
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  2. Narmina Mustafayeva
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  3. Dshavanchir Aliev
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Editor information

Editors and Affiliations

  1. US Department of Energy, Idaho Operations Office, Idaho Falls, Idaho, USA

    Mohammed K. Zaidi

  2. Institute of Radiation Problems, Azerbaijan National Academy of Sciences, Baku, Azerbaijan

    Islam Mustafaev

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© 2004 Kluwer Academic Publishers

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Alieva, I.N., Mustafayeva, N., Aliev, D. (2004). Structure of Met30-Ser40 Segment in N-Terminus of Human Tyrosine Hydroxylase Type1. In: Zaidi, M.K., Mustafaev, I. (eds) Radiation Safety Problems in the Caspian Region. Nato Science Series: IV: Earth and Environmental Sciences, vol 41. Springer, Dordrecht. https://doi.org/10.1007/1-4020-2378-2_10

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