2bo5: Difference between revisions
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[[Image:2bo5. | {{Seed}} | ||
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{{STRUCTURE_2bo5| PDB=2bo5 | SCENE= }} | {{STRUCTURE_2bo5| PDB=2bo5 | SCENE= }} | ||
===BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN=== | |||
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The | The line below this paragraph, {{ABSTRACT_PUBMED_16045926}}, adds the Publication Abstract to the page | ||
(as it appears on PubMed at http://www.pubmed.gov), where 16045926 is the PubMed ID number. | |||
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{{ABSTRACT_PUBMED_16045926}} | |||
==About this Structure== | ==About this Structure== | ||
2BO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full | 2BO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Transit peptide]] | [[Category: Transit peptide]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:57:22 2008'' | |||
Revision as of 22:57, 28 July 2008
BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN
Template:ABSTRACT PUBMED 16045926
About this Structure
2BO5 is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.
Reference
Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit., Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D, J Mol Biol. 2005 Aug 26;351(4):824-38. PMID:16045926
Page seeded by OCA on Tue Jul 29 01:57:22 2008
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Pages with broken file links
- Bos taurus
- Single protein
- Carbajo, R J.
- Kellas, F A.
- Montgomery, M G.
- Neuhaus, D.
- Runswick, M J.
- Walker, J E.
- Alpha-subunit
- Atp synthase
- Beta-subunit
- Binding interface
- Chemical shift mapping
- Chemical shift perturbation
- Hydrogen ion transport
- Hydrolase
- Ion transport
- Mitochondrion
- Nmr
- Oscp
- Peripheral stalk
- Protein-protein interaction
- Titration
- Transit peptide
- Transport