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NMR Investigation about Heterogeneous Structure and Dynamics of Recombinant Spider Silk in the Dry and Hydrated States.

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Title: NMR Investigation about Heterogeneous Structure and Dynamics of Recombinant Spider Silk in the Dry and Hydrated States.
Authors: Yugo Tasei1, Akio Nishimura1, Yu Suzuki2, Sato, Takehiro K.3, Junichi Sugahara3, Tetsuo Asakura1 asakura@cc.tuat.ac.jp
Source: Macromolecules. 10/24/2017, Vol. 50 Issue 20, p8117-8128. 12p.
Subjects: Spider silk, Recombinant proteins, Polyalanine, Hydrates, Nuclear magnetic resonance spectroscopy, Molecular structure
Abstract: Spider silks continue to attract researchers because of their excellent mechanical properties and supercontraction behavior. In this paper, the structure and dynamics of recombinant spider silk protein (RSP) were characterized using 13C CP/MAS, 13C DD/MAS, and 13C refocused-INEPT NMR spectroscopies in the dry and hydrated states. The fractions of several structures of RSP with helical, random coil, and β-sheet polyalanine sequences were determined from the CP/MAS NMR spectra in the dry state. The CP/MAS NMR spectra changed to very simple one with dominant β-sheet Ala peaks by hydration due to a significant loss in CP signals of the other mobile carbons. On the contrary, only sharp mobile peaks, and both mobile and immobile peaks could be observed in the refocused-INEPT and DD/MAS NMR spectra, respectively. The cis/trans proportion of the Gly-Pro bond was also determined. Our measurements provide new insight into understanding the supercontraction phenomenon of spider silks. [ABSTRACT FROM AUTHOR]
Copyright of Macromolecules is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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DbLabel: Engineering Source
An: 125909157
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Items – Name: Title
  Label: Title
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  Data: NMR Investigation about Heterogeneous Structure and Dynamics of Recombinant Spider Silk in the Dry and Hydrated States.
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  Data: <searchLink fieldCode="AR" term="%22Yugo+Tasei%22">Yugo Tasei</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Akio+Nishimura%22">Akio Nishimura</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Yu+Suzuki%22">Yu Suzuki</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Sato%2C+Takehiro+K%2E%22">Sato, Takehiro K.</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Junichi+Sugahara%22">Junichi Sugahara</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Tetsuo+Asakura%22">Tetsuo Asakura</searchLink><relatesTo>1</relatesTo><i> asakura@cc.tuat.ac.jp</i>
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  Data: <searchLink fieldCode="JN" term="%22Macromolecules%22">Macromolecules</searchLink>. 10/24/2017, Vol. 50 Issue 20, p8117-8128. 12p.
– Name: Subject
  Label: Subjects
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  Data: <searchLink fieldCode="DE" term="%22Spider+silk%22">Spider silk</searchLink><br /><searchLink fieldCode="DE" term="%22Recombinant+proteins%22">Recombinant proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Polyalanine%22">Polyalanine</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrates%22">Hydrates</searchLink><br /><searchLink fieldCode="DE" term="%22Nuclear+magnetic+resonance+spectroscopy%22">Nuclear magnetic resonance spectroscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+structure%22">Molecular structure</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Spider silks continue to attract researchers because of their excellent mechanical properties and supercontraction behavior. In this paper, the structure and dynamics of recombinant spider silk protein (RSP) were characterized using 13C CP/MAS, 13C DD/MAS, and 13C refocused-INEPT NMR spectroscopies in the dry and hydrated states. The fractions of several structures of RSP with helical, random coil, and β-sheet polyalanine sequences were determined from the CP/MAS NMR spectra in the dry state. The CP/MAS NMR spectra changed to very simple one with dominant β-sheet Ala peaks by hydration due to a significant loss in CP signals of the other mobile carbons. On the contrary, only sharp mobile peaks, and both mobile and immobile peaks could be observed in the refocused-INEPT and DD/MAS NMR spectra, respectively. The cis/trans proportion of the Gly-Pro bond was also determined. Our measurements provide new insight into understanding the supercontraction phenomenon of spider silks. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Macromolecules is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1021/acs.macromol.7b01862
    Languages:
      – Code: eng
        Text: English
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      Pagination:
        PageCount: 12
        StartPage: 8117
    Subjects:
      – SubjectFull: Spider silk
        Type: general
      – SubjectFull: Recombinant proteins
        Type: general
      – SubjectFull: Polyalanine
        Type: general
      – SubjectFull: Hydrates
        Type: general
      – SubjectFull: Nuclear magnetic resonance spectroscopy
        Type: general
      – SubjectFull: Molecular structure
        Type: general
    Titles:
      – TitleFull: NMR Investigation about Heterogeneous Structure and Dynamics of Recombinant Spider Silk in the Dry and Hydrated States.
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            NameFull: Yugo Tasei
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            NameFull: Akio Nishimura
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            NameFull: Yu Suzuki
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            NameFull: Sato, Takehiro K.
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            NameFull: Junichi Sugahara
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            NameFull: Tetsuo Asakura
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            – D: 24
              M: 10
              Text: 10/24/2017
              Type: published
              Y: 2017
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              Value: 50
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