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Volumn 493, Issue 2, 2010, Pages 207-212

Intrinsic hTRF1 fluorescence quenching reveals details of telomere DNA binding activity: Impact of DNA length, structure and position of telomeric repeats

(2) Tahmaseb, Kambiz a Turchi, John J b

a WRIGHT STATE UNIVERSITY (United States)

b INDIANA UNIVERSITY SCHOOL OF MEDICINE (United States)

Author keywords

c myb; DNA binding; Fluorescence quenching; Kinetics; Pre steady state; TRF1

Indexed keywords

DNA; TELOMERIC REPEAT BINDING FACTOR 1; TRYPTOPHAN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING ASSAY; BINDING KINETICS; BINDING SITE; CONTROLLED STUDY; DNA STRUCTURE; FLUORESCENCE; HUMAN; MOLECULAR RECOGNITION; NONHUMAN; POSITION EFFECT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN PURIFICATION; STRUCTURE ANALYSIS; TELOMERE;

ANIMALS; DNA; FLUORESCENCE; HUMANS; KINETICS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; REPETITIVE SEQUENCES, NUCLEIC ACID; TELOMERE; TELOMERIC REPEAT BINDING PROTEIN 1;

EID: 72949107605 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2009.10.015 Document Type: Article

Times cited : (4)

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