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Cooperative Unfolding of Residual Structure in Heat Denatured Proteins by Urea and Guanidinium Chloride
The denatured states of proteins have always attracted our attention due to the fact that the denatured state is the only experimentally achievable state of a protein, which can be taken as initial reference state for considering the in vitro folding and defining the native protein stability. It is...
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| Vydáno v: | PLoS One |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Public Library of Science
2015
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4457810/ https://ncbi.nlm.nih.gov/pubmed/26046628 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0128740 |
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