Dynamics of nucleotide incorporation: snapshots revealed by 2-aminopurine fluorescence studies.
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Kinetics of Mismatch Formation opposite Lesions by the Replicative DNA Polymerase from Bacteriophage RB69Structure of the 2-Aminopurine-Cytosine Base Pair Formed in the Polymerase Active Site of the RB69 Y567A-DNA PolymeraseUsing a Fluorescent Cytosine Analogue tC o To Probe the Effect of the Y567 to Ala Substitution on the Preinsertion Steps of dNMP Incorporation by RB69 DNA PolymeraseThe E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide SelectionIdentification of a new motif in family B DNA polymerases by mutational analyses of the bacteriophage t4 DNA polymerase.RB69 DNA polymerase structure, kinetics, and fidelity.Effect of N2-guanyl modifications on early steps in catalysis of polymerization by Sulfolobus solfataricus P2 DNA polymerase Dpo4 T239W.The reopening rate of the fingers domain is a determinant of base selectivity for RB69 DNA polymerase.Effect of A and B metal ion site occupancy on conformational changes in an RB69 DNA polymerase ternary complex.Engineering processive DNA polymerases with maximum benefit at minimum costDNA conformational changes at the primer-template junction regulate the fidelity of replication by DNA polymerase.Site-specific labeling of T7 DNA polymerase with a conformationally sensitive fluorophore and its use in detecting single-nucleotide polymorphisms.Characterization and use of an unprecedentedly bright and structurally non-perturbing fluorescent DNA base analogue.Use of 2-aminopurine fluorescence to study the role of the beta hairpin in the proofreading pathway catalyzed by the phage T4 and RB69 DNA polymerasesDirect observation of translocation in individual DNA polymerase complexes.Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates.Quantitative sampling of conformational heterogeneity of a DNA hairpin using molecular dynamics simulations and ultrafast fluorescence spectroscopyIdentifying the features of purine dNTPs that allow accurate and efficient DNA replication by herpes simplex virus I DNA polymerase.Multisubunit RNA polymerases melt only a single DNA base pair downstream of the active site.Different Divalent Cations Alter the Kinetics and Fidelity of DNA Polymerases.Mechano-chemical kinetics of DNA replication: identification of the translocation step of a replicative DNA polymerase.A mechanism of nucleotide misincorporation during transcription due to template-strand misalignment.DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase.
P2860
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P2860
Dynamics of nucleotide incorporation: snapshots revealed by 2-aminopurine fluorescence studies.
description
2006 nî lūn-bûn
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
@zh-hk
2006年論文
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2006年論文
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2006年论文
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2006年论文
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2006年论文
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name
Dynamics of nucleotide incorpo ...... nopurine fluorescence studies.
@en
type
label
Dynamics of nucleotide incorpo ...... nopurine fluorescence studies.
@en
prefLabel
Dynamics of nucleotide incorpo ...... nopurine fluorescence studies.
@en
P2093
P2860
P356
P1433
P1476
Dynamics of nucleotide incorpo ...... nopurine fluorescence studies.
@en
P2093
Chithra Hariharan
Eric T Kool
Linda B Bloom
Linda J Reha-Krantz
Sandra A Helquist
P2860
P304
P356
10.1021/BI051644S
P407
P577
2006-03-01T00:00:00Z