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https://doi.org/10.1007/978-1-4302-0477-0des to facilitate protein folding in vivo and in vitro under nonideal or stressful conditions (., .). A variety of methods have been used to assess substrate protein binding to the bacterial chaperonin GroEL qualitatively. One of the earliest and most popular approaches involves the inhibition of inPanther 发表于 2025-3-27 08:12:53
Practical Apache Struts 2 Web 2.0 Projectsbilize unfolded polypeptides at various levels of conformational compactness (., .). Depending on the substrate, different chaperone systems are required to allow folding to the native state. Some proteins fold with high yields in a chaperone-unassisted reaction (., .) whereas other proteins exhibit昏睡中 发表于 2025-3-27 12:37:44
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AppRun Development Environment,Hsp60 (also known as chaperonin-60) cpn60, in the presence of ATP, thereby promoting a conformational change in Hsp60 and enclosing the protein substrate within the complex (.). ATP hydrolysis by Hsp60 destabilizes the Hsp60/ Hsp10 complex, allowing it to dissociate and release the substrate proteininculpate 发表于 2025-3-28 08:14:13
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