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Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding
The amino acid substitution or post-translational modification of a cytosolic protein can cause unpredictable changes to its electrophoretic mobility during SDS-PAGE. This type of “gel shifting” has perplexed biochemists and biologists for decades. We identify a mechanism for “gel shifting” that pre...
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| Autori principali: | , , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Wiley Subscription Services, Inc., A Wiley Company
2012
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3537240/ https://ncbi.nlm.nih.gov/pubmed/22692797 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2107 |
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