Novel type of enzyme multimerization enhances substrate affinity of oat 
beta-glucosidase

Kim, S. Y.; Kim, Y. W.; Hegerl, R.; Cyrklaff, M.; Kim, I. S.

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Novel type of enzyme multimerization enhances substrate affinity of oat beta-glucosidase

Kim, S. Y., Kim, Y. W., Hegerl, R., Cyrklaff, M., & Kim, I. S. (2005). Novel type of enzyme multimerization enhances substrate affinity of oat beta-glucosidase. Journal of Structural Biology, 150(1), 1-10.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-667C-5 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-667D-3

Genre: Journal Article

Alternative Title : J. Struct. Biol.

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Creators:
Kim, S. Y., Author
Kim, Y. W., Author
Hegerl, R.¹, Author
Cyrklaff, M.¹, Author
Kim, I. S., Author

Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142

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Free keywords: cryo-electron microscopy; cryo-negative staining; fibrillar multimer; beta-glucosidase; hexamer; oat; substrate affinity

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Language(s): eng - English

Dates: Date issued: 2005-04

Publication Status: Issued

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Rev. Type: Peer

Identifiers: eDoc: 261747
ISI: 000228196500001

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Title: Journal of Structural Biology

Alternative Title : J. Struct. Biol.

Source Genre: Journal

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Pages: - Volume / Issue: 150 (1) Sequence Number: - Start / End Page: 1 - 10 Identifier: ISSN: 1047-8477