Thermodynamic analysis of the structure-function relationship in the total DNA-binding site of enzyme-DNA complexes
about
Energetics of the Escherichia coli DnaT protein trimerization reaction.SAMHD1 is a single-stranded nucleic acid binding protein with no active site-associated nuclease activityMacromolecular competition titration method accessing thermodynamics of the unmodified macromolecule-ligand interactions through spectroscopic titrations of fluorescent analogs.The N-terminal domain of the Escherichia coli PriA helicase contains both the DNA- and nucleotide-binding sites. Energetics of domain--DNA interactions and allosteric effect of the nucleotide cofactorsInteractions of the DNA polymerase X from African Swine Fever Virus with the ssDNA. Properties of the total DNA-binding site and the strong DNA-binding subsite.The Escherichia coli primosomal DnaT protein exists in solution as a monomer-trimer equilibrium systemQuantitative Thermodynamic Analyses of Spectroscopic Titration Curves.The primary DNA-binding subsite of the rat pol β. Energetics of interactions of the 8-kDa domain of the enzyme with the ssDNA
P2860
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P2860
Thermodynamic analysis of the structure-function relationship in the total DNA-binding site of enzyme-DNA complexes
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Thermodynamic analysis of the ...... g site of enzyme-DNA complexes
@en
type
label
Thermodynamic analysis of the ...... g site of enzyme-DNA complexes
@en
prefLabel
Thermodynamic analysis of the ...... g site of enzyme-DNA complexes
@en
P2860
P1476
Thermodynamic analysis of the ...... g site of enzyme-DNA complexes
@en
P2093
Maria J Jezewska
Wlodzimierz Bujalowski
P2860
P304
P356
10.1016/S0076-6879(09)66013-4
P407
P577
2009-01-01T00:00:00Z