Kinetics and thermodynamics of salt-dependent T7 gene 2.5 protein binding to single- and double-stranded DNA - Wikidata - wikimedia - TriplyDB

Kinetics and thermodynamics of salt-dependent T7 gene 2.5 protein binding to single- and double-stranded DNA

Kinetics and thermodynamics of salt-dependent T7 gene 2.5 protein binding to single- and double-stranded DNA

http://www.wikidata.org/entity/Q36909335

about

C-terminal domain modulates the nucleic acid chaperone activity of human T-cell leukemia virus type 1 nucleocapsid protein via an electrostatic mechanism.Interaction of bacteriophage T4 and T7 single-stranded DNA-binding proteins with DNA.Biophysical characterization of DNA binding from single molecule force measurements Single-molecule stretching studies of RNA chaperones.Single-molecule views of protein movement on single-stranded DNA.Optical tweezers experiments resolve distinct modes of DNA-protein binding.C-terminal phenylalanine of bacteriophage T7 single-stranded DNA-binding protein is essential for strand displacement synthesis by T7 DNA polymerase at a nick in DNA.Feeling inter- or intramolecular interactions with the polymer chain as probe: recent progress in SMFS studies on macromolecular interactions.Denaturation transition of stretched DNA.Optical manipulation of single molecules in the living cell.Structural Basis for DNA Recognition of a Single-stranded DNA-binding Protein from Enterobacter Phage Enc34.Gp2.5, the multifunctional bacteriophage T7 single-stranded DNA binding protein

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P2860

Kinetics and thermodynamics of salt-dependent T7 gene 2.5 protein binding to single- and double-stranded DNA

http://www.wikidata.org/entity/Q36909335

description

2008 nî lūn-bûn

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Nucleic Acids Research

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Kinetics and thermodynamics of ...... ingle- and double-stranded DNA

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Andreas Hanke

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Boriana Marintcheva

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Ioulia Rouzina

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Leila Shokri

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Mootaz Eldib

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P2860

Structure of the DNA binding domain of E. coli SSB bound to ssDNA

Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7

Exploring the interaction of ruthenium(II) polypyridyl complexes with DNA using single-molecule techniques.

A distinctive single-strand DNA-binding protein from the Archaeon Sulfolobus solfataricus.

Essential amino acid residues in the single-stranded DNA-binding protein of bacteriophage T7. Identification of the dimer interface.

Microsecond dynamics of protein-DNA interactions: direct observation of the wrapping/unwrapping kinetics of single-stranded DNA around the E. coli SSB tetramer.

T7 single strand DNA binding protein but not T7 helicase is required for DNA double strand break repair.

Effect of pH on the overstretching transition of double-stranded DNA: evidence of force-induced DNA melting.

Force-induced melting of the DNA double helix. 2. Effect of solution conditions.

Target search of N sliding proteins on a DNA

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5668-5677

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10.1093/NAR/GKN551

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17

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36

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Mark C. Williams

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23238322

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18772224

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2553585

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