טוען...
Precise Binding of Tropomyosin on Actin Involves Sequence-Dependent Variance in Coiled-Coil Twisting
Often considered an archetypal dimeric coiled coil, tropomyosin nonetheless exhibits distinctive “noncanonical” core residues located at the hydrophobic interface between its component α-helices. Notably, a charged aspartate, D137, takes the place of nonpolar residues otherwise present. Much specula...
שמור ב:
| הוצא לאור ב: | Biophys J |
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| Main Authors: | , , , , , , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
The Biophysical Society
2018
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6139885/ https://ncbi.nlm.nih.gov/pubmed/30195938 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2018.08.017 |
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