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Flavodoxin Cofactor Binding Induces Structural Changes that are Required for Protein-Protein Interactions with NADP(+) Oxidoreductase and Pyruvate Formate-Lyase Activating Enzyme
Flavodoxin (Fld) conformational changes, thermal stability, and cofactor binding were studied using circular dichroism (CD), isothermal titration calorimetry (ITC), and limited proteolysis. Thermodynamics of apo and holo-Fld folding were examined to discern the features of this important electron tr...
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| Huvudupphovsmän: | , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
2013
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4012331/ https://ncbi.nlm.nih.gov/pubmed/24016774 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbapap.2013.08.014 |
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