Autor: |
Osmanovic, Dino, Rabin, Yitzhak |
Rok vydání: |
2017 |
Předmět: |
|
Druh dokumentu: |
Working Paper |
DOI: |
10.1016/j.bpj.2017.08.062 |
Popis: |
A significant part of the proteome is composed of intrinsically-disordered proteins (IDPs). These proteins do not fold into a well-defined structure and behave like ordinary polymers. In this work we consider IDPs which have the tendency to aggregate, model them as heteropolymers that contain a small number of associating monomers and use computer simulations in order to compare the aggregation of such IDPs that are grafted to a surface or free in solution. We then discuss how such grafting may affect the analysis of in-vitro experiments and could also be used to suppress harmful aggregation. |
Databáze: |
arXiv |
Externí odkaz: |
|