DocumentCode :
2930547
Title :
Single molecule fluorescence study of DNA helicase activity
Author :
Ha, Taehoon ; Babcock, H.P. ; Cheng, William ; Lohman, T.M. ; Chu, S.
Author_Institution :
Dept. of Phys., Stanford Univ., CA, USA
fYear :
2000
fDate :
7-12 May 2000
Firstpage :
589
Lastpage :
590
Abstract :
Summary form only given. DNA helicases are essential enzymes that unwind double stranded (ds) DNA to generate the single stranded (ss) DNA intermediates needed for DNA replication, repair and recombination. Helicases consume fuel molecules such as ATP to move along DNA and unwind it processively; hence they are considered "motor proteins." We are investigating the molecular mechanism of helicases at the single molecule level using fluorescence resonance energy transfer (FRET) between two dyes, donor and acceptor, specifically attached to opposite strands of a dsDNA. FRET efficiency thus measured is an indicator of the distance between two dyes, revealing the extent and the time-course of unwinding.
Keywords :
DNA; fluorescence; molecular biophysics; proteins; ATP; DNA helicase activity; DNA helicases; DNA recombination; DNA repair; DNA replication; DNA unwinding; acceptor; distance; donor; double stranded DNA; dyes; enzymes; fluorescence resonance energy transfer; fuel molecules; molecular mechanism; motor proteins; single molecule fluorescence study; single molecule level; single stranded DNA; time-course; unwinding; unwinding DNA; Biochemistry; DNA; Energy exchange; Fluorescence; Fuels; Proteins; Resonance;
fLanguage :
English
Publisher :
ieee
Conference_Titel :
Lasers and Electro-Optics, 2000. (CLEO 2000). Conference on
Conference_Location :
San Francisco, CA, USA
Print_ISBN :
1-55752-634-6
Type :
conf
DOI :
10.1109/CLEO.2000.907430
Filename :
907430
Link To Document :
بازگشت