Tthssb
WebMay 17, 2006 · We have overexpressed the native and mutant forms of TthSSB protein in Escherichia coli and purified them to homogeneity. In vitro, these proteins were found to … WebNov 15, 2003 · The presence of TthSSB increased the fidelity of the proof- reading-free DNA polymerase of T.thermophilus. TthSSB was also able to bind single-stranded RNA, …
Tthssb
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WebJul 27, 2006 · TthSSB-255 could only enhance RCA reactions drastically, which showed weak ssDNA binding affinity. This characteristic of the protein would be critical for reduction of nonspecific products. As shown in Supplementary Figure SP2, TthSSB has a significant cluster consisting of acidic residues in its C-terminus although the role has not been … Webdate, offering an attractive alternative to TaqSSB and TthSSB in molecular biology applications, especially with using high temperature e. g. polymerase chain reaction (PCR). Background Single-stranded DNA-binding (SSB) proteins play an essential role in allin vivo processes involving ssDNA. They interact with ssDNA and RNA, in an independent
WebHere we show, using single-molecule fluorescence resonance energy transfer (FRET), that homodimeric bacterial SSB from Thermus thermophilus (Tth) is able to diffuse … WebMay 12, 2009 · Use of the mutant TthSSB resulted in an enhancement of plasmid or mitochondrial DNA content in the amplified product by approximately 500x. The use of mutant TthSSB not only promoted the amplification of circular target DNA over the background but also could be used to enhance the amplification of circular targets over …
WebJun 1, 2005 · The presence of TthSSB increased the fidelity of the proof- reading-free DNA polymerase of T.thermophilus, and was also able to bind single-stranded RNA, allowing a dramatic enhancement of the reverse transcription activity of its cognate TthDNA polymerase during cDNA synthesis. Expand
WebNov 15, 2003 · The thermostability of TthSSB was also studied. To this end, TthSSB was pre‐incubated at 94°C for different times, cooled down to 70°C, and immediately …
WebAug 2, 2006 · These results were surprising in the context of half-life of SSB from thermophilic T. aquaticus, which has only 30 s of half-life at 95 degrees C. DrpSSB is the most thermostable SSB-like protein identified to date, offering an attractive alternative for TaqSSB and TthSSB in their applications for molecular biology methods and analytical … flynn engineering servicesWebDespite this, the ®delity of the Tth DNA polymerase in the presence of TthSSB in these assays was an order of magnitude lower than that obtained with the proof-reading … flynn enemy at the gatesWebJun 21, 2006 · It is shown that DgeSSB is similar to Thermus/Deinococcus SSB in its biochemical properties and offers an attractive alternative for TaqSSB and TthSSB in their applications for molecular biology methods and for analytical purposes. To study the biochemical properties of single-stranded DNA-binding (SSB) protein from Deinococcus … flynn estherWebfrom T.thermophilus strain HB8 (TthSSB) increases the effi-*To whom correspondence should be addressed. Tel: +81 45 508 7224; Fax: +81 45 508 7364; Email: [email protected] The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors The Author 2006. Published by Oxford University Press. green out pure xl - amnesia hazeWebNov 15, 2003 · The thermostability of TthSSB was also studied. To this end, TthSSB was pre‐incubated at 94°C for different times, cooled down to 70°C, and immediately subjected to bandshift assays. As shown in Figure 2 C, TthSSB could withstand up to 2 min incubation at 94°C, without any detectable loss of its ssDNA‐specific binding activity. flynn esther producerWebThe N-terminal domain is located in the region from amino acid 1 to 123 and the C-terminal domain is located between amino acids 124 and 264 or 266 in TthSSB and TaqSSB, … flynn e scooterWebOct 1, 2002 · The nucleotide (nt) sequence revealed that T. thermophilus SSB (TthSSB) and T. aquaticus (TaqSSB) consist of 264 and 266 amino acids, respectively, and have a molecular weight of 29.87 and 30.03kDa, respectively. The homology between these protein, is very high-82% identity and 90% similarity. They are the largest known prokaryotic SSB … flynnestore.com