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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...

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High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
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Quantifying multiscale noise sources in single-molecule time series.

Christopher P Calderon1, Nolan C Harris, Ching-Hwa Kiang

  • 1Department of Computational & Applied Mathematics, Rice University, Houston, Texas 77005-1892, USA. calderon@rice.edu

The Journal of Physical Chemistry. B
|December 17, 2008
PubMed
Summary

We developed methods to analyze single-molecule data by calibrating models from time series. This allows for noise quantification and understanding complex dynamics in experiments like protein unfolding.

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Area of Science:

  • Biophysics
  • Statistical Mechanics
  • Computational Biology

Background:

  • Single-molecule data analysis often relies on low-dimensional observables.
  • Stochastic dynamical models are crucial for interpreting time-series data from single-molecule experiments.

Purpose of the Study:

  • To demonstrate numerical techniques for quantifying noise across multiple timescales in single trajectories.
  • To apply these techniques to analyze the mechanical unfolding of titin's I27 domain from both simulations and experiments.
  • To enable various applications of calibrated models for deeper insights into molecular dynamics.

Main Methods:

  • Calibration of stochastic dynamical models using time-series data of system observables.
  • Numerical quantification of experimental instrument noise and inherent thermal noise.
  • Application to analyze nonequilibrium mechanical unfolding of titin's I27 domain.

Main Results:

  • Developed methods to quantify noise sources, including instrument and thermal noise.
  • Applied techniques to single-molecule data from titin I27 unfolding experiments and simulations.
  • Demonstrated model utility for detecting rare events, assessing conformational influences, and comparing noise sources.

Conclusions:

  • Calibrated stochastic models provide a powerful framework for analyzing complex single-molecule dynamics.
  • The developed techniques facilitate quantitative comparison of different noise sources.
  • These methods enhance the interpretation of experimental data and enable hypothesis testing for molecular systems.