Analyzing single-molecule manipulation experiments.
Single-molecule manipulation studies can provide quantitative information about the physical properties of complex biological molecules without ensemble artifacts obscuring the measurements. We demonstrate computational techniques which aim at more fully utilizing the wealth of information contained in noisy experimental time series. The "noise" comes from multiple sources e.g., inherent thermal motion, instrument measurement error, etc. The primary focus of this paper is a methodology that uses time domain based methods to extract the effective molecular friction from single-molecule pulling data. We studied molecules composed of eight tandem repeat titin I27 domains, but the modeling approaches have applicability to other single-molecule mechanical studies. The merits and challenges associated with applying such a computational approach to existing single-molecule manipulation data are also discussed.
Calderon
Christopher P
CP
Department of Computational and Applied Mathematics, Rice University, Houston, TX 77005, USA. calderon@rice.edu
Harris
Nolan C
NC
Kiang
Ching-Hwa
CH
Cox
Dennis D
DD
D003198:Computer Simulation; D064211:Connectin; D006801:Humans; D016013:Likelihood Functions; D018625:Microscopy, Atomic Force; D008968:Molecular Conformation; D009124:Muscle Proteins / Q000737:chemistry; D011494:Protein Kinases / Q000737:chemistry
D064211:Connectin; D009124:Muscle Proteins; C577285:TTN protein, human; D011494:Protein Kinases