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Substrate Binding Tunes Conformational Flexibility and Kinetic Stability of an Amino Acid Antiporter
We used single molecule dynamic force spectroscopy to unfold individual serine/threonine antiporters SteT from Bacillus subtilis. The unfolding force patterns revealed interactions and energy barriers that stabilized structural segments of SteT. Substrate binding did not establish strong localized i...
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| Main Authors: | , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2009
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2707244/ https://ncbi.nlm.nih.gov/pubmed/19419962 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.004267 |
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