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Structural Comparison of the Two Alternative Transition States for Folding of TI I27

TI I27, a β-sandwich domain from the human muscle protein titin, has been shown to fold via two alternative pathways, which correspond to a change in the folding mechanism. Under physiological conditions, TI I27 folds by a classical nucleation-condensation mechanism (diffuse transition state), where...

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Hlavní autoři: Geierhaas, Christian D., Best, Robert B., Paci, Emanuele, Vendruscolo, Michele, Clarke, Jane
Médium: Artigo
Jazyk:Inglês
Vydáno: Biophysical Society 2006
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1479071/
https://ncbi.nlm.nih.gov/pubmed/16603501
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.105.077057
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