Journal article
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b-type variant
- Abstract:
-
© 2015 The Author(s). Cytochrome c
Expand abstract552 from the thermophilic bacterium Hydrogenobacter thermophilus is a typical c-type cytochrome which binds heme covalently via two thioether bonds between the two heme vinyl groups and two cysteine thiol groups in a CXXCH sequence motif. This protein was converted to a b-type cytochrome by substitution of the two cysteine residues by alanines (Tomlinson and Ferguson in Proc Natl Acad Sci USA 97:5156-5160, 2000a). To probe the significance of the ...
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Version of record, pdf, 1.0MB)
-
- Publisher copy:
- 10.1007/s10858-015-9938-3
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Funding
Bibliographic Details
- Publisher:
- Springer Verlag Publisher's website
- Journal:
- Journal of Biomolecular NMR Journal website
- Volume:
- 62
- Issue:
- 2
- Pages:
- 221-231
- Publication date:
- 2015-05-08
- DOI:
- EISSN:
-
1573-5001
- ISSN:
-
0925-2738
- Source identifiers:
-
527989
Item Description
- Keywords:
- Pubs id:
-
pubs:527989
- UUID:
-
uuid:c8138965-f1fd-4c44-b0e7-7dc1f635087e
- Local pid:
- pubs:527989
- Deposit date:
- 2016-02-08
Terms of use
- Copyright holder:
- Tozawa et al
- Copyright date:
- 2015
- Notes:
- © The Author(s) 2015. This article is published with open access at Springerlink.com. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License. This is the publisher's version of the article. The final version is available online from Springer Verlag at: [10.1007/s10858-015-9938-3]
- Licence:
- CC Attribution (CC BY)
If you are the owner of this record, you can report an update to it here: Report update to this record