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Effects of Tryptophan Microenvironment, Soluble Domain, and Vesicle Size on the Thermodynamics of Membrane Protein Folding: Lessons from the Transmembrane Protein OmpA
Refolding curves of the integral membrane protein Outer Membrane Protein A (OmpA) were measured to determine the conformational stabilities of this model system for membrane protein folding. Wild-type OmpA exhibits a free energy of unfolding ( [Formula: see text]) of 10.5 kcal/mol. Mutants, containi...
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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2008
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2724591/ https://ncbi.nlm.nih.gov/pubmed/18991402 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi800860k |
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