Abstract：
:Although tertiary folding of whole protein domains is prohibited by the cramped dimensions of the ribosomal tunnel, dynamic tertiary interactions may permit folding of small elementary units within the tunnel. To probe this possibility, we used a beta-hairpin and an alpha-helical hairpin from the cytosolic N terminus of a voltage-gated potassium channel and determined a probability of folding for each at defined locations inside and outside the tunnel. Minimalist tertiary structures can form near the exit port of the tunnel, a region that provides an entropic window for initial exploration of local peptide conformations. Tertiary subdomains of the nascent peptide fold sequentially, but not independently, during translation. These studies offer an approach for diagnosing the molecular basis for folding defects that lead to protein malfunction and provide insight into the role of the ribosome during early potassium channel biogenesis.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Kosolapov A,Deutsch Cdoi
10.1038/nsmb.1571subject
Has Abstractpub_date
2009-04-01 00:00:00pages
405-11issue
4eissn
1545-9993issn
1545-9985pii
nsmb.1571journal_volume
16pub_type
杂志文章abstract：:Chromatin is a dynamic structure that must respond to myriad stimuli to regulate access to DNA, and chemical modification of histones is a major means by which the cell modulates nucleosome mobility and turnover. Histone modifications are linked to essentially every cellular process requiring DNA access, including tra...
journal_title：Nature structural & molecular biology
pub_type： 杂志文章,评审
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abstract：:The DNA-damage response (DDR) ensures genome stability and proper inheritance of genetic information, both of which are essential to survival. It is presently unclear to what extent other signaling pathways modulate DDR function. Here we show that Notch receptor binds and inactivates ATM kinase and that this mechanism...
journal_title：Nature structural & molecular biology
pub_type： 杂志文章
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abstract：:An amendment to this paper has been published and can be accessed via a link at the top of the paper. ...
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb.1603
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
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更新日期：2013-05-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb.2293
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb.1625
更新日期：2009-07-01 00:00:00
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pub_type： 杂志文章
doi：10.1038/nsmb989
更新日期：2005-10-01 00:00:00
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pub_type： 杂志文章
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb.2565
更新日期：2013-05-01 00:00:00
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journal_title：Nature structural & molecular biology
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更新日期：2009-07-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
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更新日期：2014-04-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb813
更新日期：2004-09-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb866
更新日期：2004-12-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb1352
更新日期：2008-01-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
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更新日期：2008-01-01 00:00:00
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pub_type： 杂志文章
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更新日期：2004-10-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
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更新日期：2014-05-01 00:00:00
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journal_title：Nature structural & molecular biology
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更新日期：2007-12-01 00:00:00
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journal_title：Nature structural & molecular biology
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更新日期：2010-12-01 00:00:00
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更新日期：2006-09-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
doi：10.1038/nsmb.2380
更新日期：2012-10-01 00:00:00
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journal_title：Nature structural & molecular biology
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
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更新日期：2008-02-01 00:00:00
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journal_title：Nature structural & molecular biology
pub_type： 杂志文章
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