Folding and stability of integral membrane proteins in amphipols
2014; Elsevier BV; Volume: 564; Linguagem: Inglês
10.1016/j.abb.2014.10.013
ISSN1096-0384
AutoresJörg H. Kleinschmidt, Jean‐Luc Popot,
Tópico(s)RNA and protein synthesis mechanisms
ResumoAmphipols (APols) are a family of amphipathic polymers designed to keep transmembrane proteins (TMPs) soluble in aqueous solutions in the absence of detergent. APols have proven remarkably efficient at (i) stabilizing TMPs, as compared to detergent solutions, and (ii) folding them from a denatured state to a native, functional one. The underlying physical–chemical mechanisms are discussed.
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