Database error: Invalid SQL: update pwn_comment set cl=cl+1 where id='570760' and iffb='1'
MySQL Error: 996 (Query execution was interrupted, max_statement_time exceeded)
#0 dbbase_sql->halt(Invalid SQL: update pwn_comment set cl=cl+1 where id='570760' and iffb='1') called at [/www/users/HK591466/WEB/includes/db.inc.php:65] #1 dbbase_sql->query(update {P}_comment set cl=cl+1 where id='570760' and iffb='1') called at [/www/users/HK591466/WEB/comment/module/CommentContent.php:54] #2 CommentContent() called at [/www/users/HK591466/WEB/includes/common.inc.php:551] #3 printpage() called at [/www/users/HK591466/WEB/comment/html/index.php:13]
Warning: mysql_query() [function.mysql-query]: Unable to save result set in /www/users/HK591466/WEB/includes/db.inc.php on line 59
Database error: Invalid SQL: select * from pwn_comment where pid='570760' and iffb='1' order by id limit 0,10
MySQL Error: 996 (Query execution was interrupted, max_statement_time exceeded)
#0 dbbase_sql->halt(Invalid SQL: select * from pwn_comment where pid='570760' and iffb='1' order by id limit 0,10) called at [/www/users/HK591466/WEB/includes/db.inc.php:65] #1 dbbase_sql->query(select * from {P}_comment where pid='570760' and iffb='1' order by id limit 0,10) called at [/www/users/HK591466/WEB/comment/module/CommentContent.php:167] #2 CommentContent() called at [/www/users/HK591466/WEB/includes/common.inc.php:551] #3 printpage() called at [/www/users/HK591466/WEB/comment/html/index.php:13]
Warning: mysql_fetch_array(): supplied argument is not a valid MySQL result resource in /www/users/HK591466/WEB/includes/db.inc.php on line 72
网友点评-Protein interactions {and other|as well as other|along with other-缅甸银河国际-13150768882
会员登录信息
您好,欢迎光临!   [请登录]   [免费注册]
网站标志
商品搜索
点评详情
发布于:2019-6-5 12:39:12  访问:18 次 回复:0 篇
版主管理 | 推荐 | 删除 | 删除并扣分
Protein interactions {and other|as well as other|along with other
The potential of protein fragments to associate with one another can rely on the frequency of their collisions, which depends on the powerful regional SKF-102886;WR-171669COA concentrations of your fragments. In numerous situations the fragments are predicted to exist inside a partially unfolded state as a result of absence of interactions that happen to be required for formation of some secondary structure elements within the individual fragments. Unfortunately, the structures of protein fragments which will undergo co.Protein interactions along with other molecular processes in living cells (see Box
Protein interactions and other molecular processes in living cells (see Box two around the detection of protein interactions applying complementation approaches). Complementation involving fragments of various unique proteins enables detection of protein interactions in living cells. Nevertheless, visualization from the subcellular localization of protein complexes calls for that the function developed by complementation may be detected with higher spatial resolution. This is doable by using fluorescent ligands that bind towards the complementation complex or by utilizing bimolecular fluorescence complementation, which produces an intrinsically fluorescent complicated. Box two Complementation approaches for the detection of protein interactions Many proteins is often divided into fragments that can associate to make a functional complex. This phenomenon is classically known as complementation by analogy with the capability of diverse mutations to complement one another to produce an organism with a normal phenotype. Complementation amongst protein fragments is because of the big favorable totally free power of folding of most proteins plus the fact that several proteins fold in numerous stages that involve initial PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/22610350 interactions amongst neighboring amino acid residues and subsequent interactions amongst partially folded secondary structure components. Nonetheless, the terrific majority of protein fragments are unable to generate a functional complicated for the reason that of misfolding or the inability of partially folded fragments to associate with each other. Only a smaller subset of protein fragments has the prospective to associate to kind a functional complicated. Experimental applications of protein fragment complementation are hence critically dependent around the identification of fragments that can associate with one another under relevant conditions. The appropriate folding of a protein happens in competition with misfolding, which can be generally irreversible. The potential of protein fragments to associate with each other can rely on the frequency of their collisions, which will depend on the powerful neighborhood concentrations of the fragments. Therefore, the association of some protein fragments might be facilitated by tethering them in proximity to each other. The association of such fragments could be conditional on their molecular proximity even if the fragments can associate independent of tethering once they are present at sufficiently higher concentrations. The conditional association of protein fragments is a highly effective reporter of molecular proximity, and may be applied to investigate many biological processes that involve changes in molecular proximity, such as proteinNIH-PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author ManuscriptMethods Cell Biol. Author manuscript; available in PMC 2010 February 26.KerppolaPageinteractions, nucleoprotein PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/24876777 complex formation and covalent protein modifications (Hu, et al., 2002, Rackham and Brown, 2004, Fang and Kerppola, 2004, Stains, et al., 2005). Fragments of several proteins happen to be identified that could complement one another beneath particular experimental circumstances (see Table 1 to get a small subset). The nature on the fragments that may undergo complementation varies among different proteins.
共0篇回复 每页10篇 页次:1/1
共0篇回复 每页10篇 页次:1/1
我要回复
回复内容
验 证 码
看不清?更换一张
匿名发表 
当前位置
脚注信息