Probing structural heterogeneities and conformational fluctuations of biopolymers

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We study protein and nucleic acid structure and dynamics using single-molecule fluorescence resonance energy transfer measurements with alternating-laser excitation. Freely diffusing molecules are sorted into subpopulations based on stoichiometry, detecting donor and acceptor coincidence for periods over 100 {micro}s-1 ms. Faster (< 100 {micro}s) fluctuating distance distributions are studied within these subpopulations using time-resolved single photon counting measurements. We find that short double-stranded DNA (dsDNA) is more flexible than expected from persistence lengths measured on long dsDNA. We find that the electrostatic portion of the persistence length of single-stranded poly-dT varies as the ionic strength (I) to the -1/2 power ... continued below

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Laurence, T; Kong, X; Jaeger, M & Weiss, S December 15, 2004.

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We study protein and nucleic acid structure and dynamics using single-molecule fluorescence resonance energy transfer measurements with alternating-laser excitation. Freely diffusing molecules are sorted into subpopulations based on stoichiometry, detecting donor and acceptor coincidence for periods over 100 {micro}s-1 ms. Faster (< 100 {micro}s) fluctuating distance distributions are studied within these subpopulations using time-resolved single photon counting measurements. We find that short double-stranded DNA (dsDNA) is more flexible than expected from persistence lengths measured on long dsDNA. We find that the electrostatic portion of the persistence length of single-stranded poly-dT varies as the ionic strength (I) to the -1/2 power (I{sup -1/2}). Lastly, we find that the unfolded protein Chymotrypsin Inhibitor 2 (CI2) is unstructured at high denaturant. However, in the presence of folded CI2 (at lower denaturant), unfolded CI2 is more compact and displays larger distance fluctuations, possibly due to unsuccessful attempts to cross the folding barrier.

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PDF-file: 30 pages; size: 1.4 Mbytes

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  • Journal Name: Proceedings of the National Academy of Sciences of the United States of America; Journal Volume: 102; Journal Issue: 48

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  • Report No.: UCRL-JRNL-208639
  • Grant Number: W-7405-ENG-48
  • Office of Scientific & Technical Information Report Number: 875953
  • Archival Resource Key: ark:/67531/metadc877350

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  • December 15, 2004

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  • Sept. 21, 2016, 2:29 a.m.

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  • Dec. 8, 2016, 8:57 p.m.

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Laurence, T; Kong, X; Jaeger, M & Weiss, S. Probing structural heterogeneities and conformational fluctuations of biopolymers, article, December 15, 2004; Livermore, California. (digital.library.unt.edu/ark:/67531/metadc877350/: accessed September 26, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.