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

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发表于 2025-3-21 16:12:01 | 显示全部楼层 |阅读模式
书目名称Chaperonin Protocols
编辑Christine Schneider
视频video
概述Includes supplementary material:
丛书名称Methods in Molecular Biology
图书封面Titlebook: Chaperonin Protocols;  Christine Schneider Book 2000 Humana Press 2000
描述In Chaperonin Protocols, Christine Schneider has assembled a unique collection of readily reproducible protocols for the study of chaperonins, intracellular 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 assays for in vivo as well as in vitro work. Many activity assays are given for GroEL, which can also be applied to mitochrondrial Hsp60. There are also assays for the eukaryotic chaperonin TRiC and handy methods-for example, one for preparing labeled probes-that can be used for various purposes and prove helpful in numerous different procedures..Critically important to a greater understanding of such disorders as cystic fibrosis, Alzheimer‘s disease, and BSE, Chaperonin Protocols offers both novice and experienced investigators fast access to today‘s best and most productive chaperonin methods, all explained in step-by-step detail to ensure robust and reproducible results..
出版日期Book 2000
版次1
doihttps://doi.org/10.1385/1592590616
isbn_softcover978-1-61737-163-9
isbn_ebook978-1-59259-061-2Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 2000
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发表于 2025-3-21 23:14:56 | 显示全部楼层
Practical Analysis in One Variableical domain and is sequestered inside the cavity of the chaperonin owing to the binding of the cochaperonin, GroES, to the same sites on the apical domains. Release of the protein from the chaperonin occurs after ATP hydrolysis. Chaperonins are broadly further classified into two other groups based
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Undergraduate Texts in Mathematics of Gp31, indicating that the Gp31 protein possesses distinct properties that are absent in GroES (.-.). The 2.3-Å crystal shows that the tertiary and quaternary structures of the Gp31 heptamer are similar to those of GroES, despite the low amino acid sequence identity between the two proteins (14%)
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Practical Apache Struts 2 Web 2.0 Projectso assemble spontaneously from monomeric subunits (.,.). Cell-free assembly of GroEL in a Mg-ATP-dependent manner, starting from monomeric subunits, has been established, too (.,.). Like with GroES, in vitro assembly of GroEL is a reversible process, and depending on the conditions, dissociation of c
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https://doi.org/10.1007/978-1-4302-0477-0 partitions to GroEL from solution. Some of these methods have relied on the heat exchanged on polypeptide binding to GroEL (., .), on the distribution of bound and free substrates detected by ultracen- trifugation (., .), and on changes in surface plasmon resonance using BIAcore (., .) .). . (.,.,
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Practical Apache Struts 2 Web 2.0 Projectsfree into solution (.). Proteins that do not reach their native state in one round of GroES binding and ATP hydrolysis rebind to GroEL on GroES release and undergo another folding cycle. Folding in a sequestered environment, effectively preventing aggregation throughout the folding pathway, facilita
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Book 2000, and BSE, Chaperonin Protocols offers both novice and experienced investigators fast access to today‘s best and most productive chaperonin methods, all explained in step-by-step detail to ensure robust and reproducible results..
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