Fluorescence intensity, anisotropy, and transient dynamic quenching stopped-flow kinetics.

about

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions.

P2860

Q39224403-D0D84A18-BAE8-4C3C-8BC1-A58421D14C84

P2860

Fluorescence intensity, anisotropy, and transient dynamic quenching stopped-flow kinetics.

Item

http://www.wikidata.org/entity/Q44145783

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh-hant

name

Fluorescence intensity, anisot ...... enching stopped-flow kinetics.

@en

Fluorescence intensity, anisot ...... enching stopped-flow kinetics.

@nl

type

Item

label

Fluorescence intensity, anisot ...... enching stopped-flow kinetics.

@en

Fluorescence intensity, anisot ...... enching stopped-flow kinetics.

@nl

prefLabel

Fluorescence intensity, anisot ...... enching stopped-flow kinetics.

@en

Fluorescence intensity, anisot ...... enching stopped-flow kinetics.

@nl

P1476

Fluorescence intensity, anisot ...... enching stopped-flow kinetics.

@en

P2093

Maria J Jezewska

http://www.w3.org/2001/XMLSchema#string

Wlodek M Bujalowski

http://www.w3.org/2001/XMLSchema#string

P2860

Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analogues

Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A

Resolution of multiphasic reactions by the combination of fluorescence total-intensity and anisotropy stopped-flow kinetic experiments.

Thermodynamic and kinetic methods of analyses of protein-nucleic acid interactions. From simpler to more complex systems.

Kinetic mechanism of the single-stranded DNA recognition by Escherichia coli replicative helicase DnaB protein. Application of the matrix projection operator technique to analyze stopped-flow kinetics.

Time-resolved analysis of macromolecular structures during reactions by stopped-flow electrooptics.

Fluorescence quenching studies with proteins.

Ligand-induced changes in membrane-bound acetylcholine receptor observed by ethidium fluorescence. 2. Stopped-flow studies with agonists and antagonists.

Kinetics of the E. coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient, dynamic quenching stopped-flow studies of the reaction intermediates.

The E. coli replication factor DnaC protein exists in two conformations with different nucleotide binding capabilities. I. Determination of the binding mechanism using ATP and ADP fluorescent analogues.

P304

105-133

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1007/978-1-61779-806-1_6

http://www.w3.org/2001/XMLSchema#string

P407

English

P478

875

http://www.w3.org/2001/XMLSchema#string

P577

2012-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

22573438

http://www.w3.org/2001/XMLSchema#string

Fluorescence intensity, anisotropy, and transient dynamic quenching stopped-flow kinetics.

about

P2860

P2860

Fluorescence intensity, anisotropy, and transient dynamic quenching stopped-flow kinetics.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P698