Warning: mysql_query() [function.mysql-query]: Unable to save result set in D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php on line 50
Database error: Invalid SQL: select count(id) from pwn_comment where pid='538582' and iffb='1'
MySQL Error: 1194 (Table 'pwn_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select count(id) from pwn_comment where pid='538582' and iffb='1') called at [D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php:54] #1 dbbase_sql->query(select count(id) from {P}_comment where pid='538582' and iffb='1') called at [D:\wwwroot\hs21cn2043\wwwroot\comment\module\CommentContent.php:65] #2 CommentContent() called at [D:\wwwroot\hs21cn2043\wwwroot\includes\common.inc.php:551] #3 printpage() called at [D:\wwwroot\hs21cn2043\wwwroot\comment\html\index.php:13]
Warning: mysql_fetch_array(): supplied argument is not a valid MySQL result resource in D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php on line 61

Warning: mysql_query() [function.mysql-query]: Unable to save result set in D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php on line 50
Database error: Invalid SQL: select * from pwn_comment where pid='538582' and iffb='1' order by id limit 0,10
MySQL Error: 1194 (Table 'pwn_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select * from pwn_comment where pid='538582' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php:54] #1 dbbase_sql->query(select * from {P}_comment where pid='538582' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\comment\module\CommentContent.php:167] #2 CommentContent() called at [D:\wwwroot\hs21cn2043\wwwroot\includes\common.inc.php:551] #3 printpage() called at [D:\wwwroot\hs21cn2043\wwwroot\comment\html\index.php:13]
Warning: mysql_fetch_array(): supplied argument is not a valid MySQL result resource in D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php on line 61
网友点评-Oblotting using rat-线缆测高仪,超声波测高仪, 手持式测高仪-上海交通大学科技园上海野豹企业发展公司
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发布于:2018-9-14 23:42:27  访问:127 次 回复: 篇
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Oblotting using rat
To predict the tertiary structure of P66, we submitted the mature sequence to the BLU-554 1707289-21-1 TMBpro server (47), which predicted that P66 forms a -barrel structure with 24 transmembrane strands (Fig. burgdorferi cells were digested with increasing amounts of trypsin, which particularly cleaves on the carboxyl side of PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/18577702 lysine and arginine residues, the 66-kDa full-length protein was reduced to 52 kDa, the size predicted if cleavage occurs at K487 (Fig. To produce a model of P66 membrane topology, we analyzed the mature P66 amino acid sequence employing PRED-TMBB (40, 41), which utilizes 3 distinct prediction algorithms (Viterbi, N-Best, and Posterior decoding) to recognize putative transmembrane domains in protein sequences. As expected of a -barrel OMP, P66 was predicted to have either 24 membrane-spanning regions in line with the Viterbi and N-Best algorithms or 22 transmembrane strands based on the Posterior decoding algorithm (Fig. 1A). Furthermore, the N- and C-terminal regions of P66 have been predicted by all three PRED-TMBB algorithms to be positioned inside the periplasm (Fig. 1A, highlighted in green), which also istypical of -barrel-forming OMPs (66). To predict the tertiary structure of P66, we submitted the mature sequence towards the TMBpro server (47), which predicted that P66 types a -barrel structure with 24 transmembrane strands (Fig. 1B). Previous proteolysis assays have revealed that P66 has a surface-exposed, trypsin-sensitive lysine at position 487 (K487) (28). Constant with this prior observation, the K487 residue was predicted by all PRED-TMBB algorithms to become in an extracellular PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/18372395 domain spanning amino acids 459 to 498 (Fig. 1A). While TMBpro also predicted K487 to become positioned in an extracellular loop, the loop within this analysis was composed of residues 462 to 502 (Fig. 1B). Lysine residue K487 is surface exposed and also the target of trypsin degradation. Amongst the Lyme disease Borrelia isolates, the P66 amino acid sequence is effectively conserved (28). Nonetheless, preceding reports have shown that greater variability exists inside a predicted surface loop of P66 containing the K487 residue (28). When the mature P66 amino acid sequences of strains B. burgdorferi B31, B. burgdorferi JD1, B. garinii IP90, and B. garinii Pbi had been aligned, the sequences shared about 90 sequence identity involving the two borrelial genospecies. Having said that, sequence identity in the surface-exposed loop (amino acids 459 to 502) (Fig. 2A, boxed in red) was only roughly 70 . Interestingly, we observed that K487, the lysine believed to become the target of trypsin digestion, was detected only inside the B. burgdorferi sensu stricto strains (Fig. 2A, red arrow). Therefore, we sought to confirm that K487 may be the surface-exposed residue targeted by trypsin within the protease experiments. Initially, we confirmed that when intact B. burgdorferi cells were digested with escalating amounts of trypsin, which especially cleaves on the carboxyl side of PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/18577702 lysine and arginine residues, the 66-kDa full-length protein was reduced to 52 kDa, the size predicted if cleavage occurs at K487 (Fig. 2B) (28). Subsequent, we incubated B. burgdorferi B31, B. burgdorferi JD1, B. garinii IP90, and B.
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