Results 21 to 30 of about 24,101 (229)
From discovery to innovation in physiological research. [PDF]
Experimental Physiology, Volume 110, Issue 3, Page 355-357, 1 March 2025.
Zacho M.
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Succinate thiokinase from Thermus aquaticus and Halobacterium salinarium [PDF]
Both citrate synthase and succinate thiokinase occur in either a ‘large’ or ‘small’ form. The ‘large’ forms of these two enzymes have been found only in Gram‐negative bacteria, whereas Gram‐positive bacteria and eukaryotes contain the ‘small’ forms of the two.
P.D.J. Weitzman, Helen A. Kinghorn
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Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase from Thermus aquaticus. [PDF]
Joyce MA+3 more
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Recombinant production of Thermus aquaticus single-strand binding protein for usage as PCR enhancer
Single-stranded DNA-binding (SSB) proteins play an important role in DNA metabolism involving DNA replication, recombination, and repair in all living beings.
Özlem Kaplan+3 more
semanticscholar +1 more source
Anomalous Citrate Synthase from Thermus aquaticus
P.D.J. Weitzman
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A change of an aspartic acid to asparagine of Taq (Thermus aquaticus) DNA polymerase is a gain of function mutation that supports faster PCR: the extension times for PCR amplification can be 2–3 times shorter.
Wayne M. Barnes+3 more
doaj +1 more source
Oligomerization of a MutS Mismatch Repair Protein from Thermus aquaticus [PDF]
The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases. We have examined the oligomerization of a MutS protein from Thermus aquaticus that binds to heteroduplex DNAs at elevated temperatures. Analytical gel filtration, cross-linking of MutS protein with disuccinimidyl suberate, light scattering, and matrix ...
Indranil Biswas+7 more
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High‐throughput sequencing (HTS) of 16S rRNA gene amplicons provides compositional information regarding the microbial community, but not the absolute abundance of the bacteria.
Ju Yeong Kim+6 more
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The crystal structure of the Thermus aquaticus DnaB helicase monomer. [PDF]
The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly dimer, at 2.9 A resolution. DnaB is a highly flexible two domain protein.
Bailey S, Eliason WK, Steitz TA.
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Structure of the GDP-bound state of the SRP GTPase FlhF. [PDF]
This study presents the X‐ray structure of FlhF in its GDP‐bound state at a resolution of 2.28 Å, exhibiting the classical N‐ and G‐domain fold. Comparative analysis with GTP‐loaded FlhF elucidates the conformational changes associated with GTP hydrolysis.The GTPase FlhF, a signal recognition particle (SRP)‐type enzyme, is pivotal for spatial–numerical
Dornes A, Mais CN, Bange G.
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