Titlebook: Chaperonin Protocols; Christine Schneider Book 2000 Humana Press 2000

宴会

共栖

Book 2000llular proteins critical to many biological processes. Written by experienced investigators who have successfully honed their methods to a fineness, the protocols focus on the purification of chaperonins from different species along with their corresponding cofactors, and on chaperonin activity assa

Painstaking

ABIDE

etidronate

Purification of Hsp60 from ,,us to the GroEL chaperonin from . (52% identity) as shown in .. It is similar to GroEL also in its structure, as seen by electron microscopy, in that it also comprises two rings of seven identical subunits (.-.). Each subunit has a mol-wt of approx 57 kDa, making the tetradecameric complex 800 kDa.

CULP

Preparation of Recombinant Human Hsp10,60/Hsp10 complex has been described by cryo-electron microscopy (.) and X-ray crystallography (.). Subunits of both Hsp10 and Hsp60 are arranged in sevenfold symmetric rings. Hsp10 is composed of 7 10-kDa subunits, and Hsp60 is composed of fourteen 60 kDa subunits.

是贪求

Peristalsis

BAIT

Purification of Yeast Mitochondrial Hsp60, (.). The ATPase rate of yeast hsp60 based on protomer at 25°C is 2.5 min.. ATP hydroloysis is reduced to approximately half of this value by the cochaperonin hsp10 that binds to hsp60 in the presence of adenosine nucleotide. Hsp60 mediates the refolding; of mammalian mitochondrial malate dehydrogenase in vitro (.).

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Practical Apache Struts 2 Web 2.0 ProjectsIn this chapter, we describe assays that can be used to determine whether or not different chaperonin proteins (either mutant forms of GroEL and GroES or “putative” chaperonins from other organisms) are able to function in . The advantage of using . for such studies is: