PROTEIN SCIENCE - Journal - Bridge of Knowledge

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PROTEIN SCIENCE

ISSN:

0961-8368

eISSN:

1469-896X

Disciplines
(Field of Science):

  • information and communication technology (Engineering and Technology)
  • biomedical engineering (Engineering and Technology)
  • medical biology (Medical and Health Sciences )
  • pharmacology and pharmacy (Medical and Health Sciences )
  • medical sciences (Medical and Health Sciences )
  • health sciences (Medical and Health Sciences )
  • agriculture and horticulture (Agricultural sciences)
  • food and nutrition technology (Agricultural sciences)
  • biotechnology (Natural sciences)
  • biological sciences (Natural sciences)
  • chemical sciences (Natural sciences)

Ministry points: Help

Ministry points - current year
Year Points List
Year 2024 100 Ministry scored journals list 2024
Ministry points - previous years
Year Points List
2024 100 Ministry scored journals list 2024
2023 100 Ministry Scored Journals List
2022 100 Ministry Scored Journals List 2019-2022
2021 100 Ministry Scored Journals List 2019-2022
2020 100 Ministry Scored Journals List 2019-2022
2019 100 Ministry Scored Journals List 2019-2022
2018 25 A
2017 25 A
2016 25 A
2015 25 A
2014 25 A
2013 25 A
2012 25 A
2011 25 A
2010 27 A

Model:

Hybrid

Points CiteScore:

Points CiteScore - current year
Year Points
Year 2023 12.4
Points CiteScore - previous years
Year Points
2023 12.4
2022 10.8
2021 12.3
2020 7.5
2019 5.4
2018 4.6
2017 4.6
2016 5
2015 5.3
2014 5.5
2013 5.5
2012 5.3
2011 5.3

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total: 3

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Catalog Journals

Year 2023
Year 2004
  • A mobile loop order–disorder transition modulates the speed of chaperonin cycling
    Publication
    • F. Shewmaker
    • M. J. Kerner
    • M. Hayer-Hartl
    • G. Klein-Raina
    • C. Georgopoulos
    • S. J. Landry

    - PROTEIN SCIENCE - Year 2004

    Molecular machines order and disorder polypeptides as they form and dissolve large intermolecular interfaces, but the biological significance of coupled ordering and binding has been established in few, if any, macromolecular systems. The ordering and binding of GroES co-chaperonin mobile loops accompany an ATP-dependent conformational change in the GroEL chaperonin that promotes client protein folding. Following ATP hydrolysis,...

    Full text available to download

Year 2000

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