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contributor authorDeman Tang
contributor authorEarl H. Dowell
date accessioned2017-05-09T00:12:35Z
date available2017-05-09T00:12:35Z
date copyrightSeptember, 2004
date issued2004
identifier issn0022-0434
identifier otherJDSMAA-26333#531_1.pdf
identifier urihttp://yetl.yabesh.ir/yetl/handle/yetl/129761
description abstractDynamic analysis and numerical simulation of a protein-ligand chain structure connected to a moving atomic force microscope (AFM) has been conducted. The elements of the chain are free to extend and rotate relative to each other in a two-dimensional plane. Sinusoidal base excitation of the cantilevered beam of the AFM is considered in some detail. Reduced order (dynamic) models are constructed using global modes for both linear and nonlinear dynamic systems with and without the “nearest neighbor assumption.” The agreement between the original and reduced order models (ROM) is very good even when only one global mode is included in the ROM for either the linear case or for the nonlinear case, provided the excitation frequency is lower than the fundamental natural frequency of the linear system. For higher excitation frequencies, more global modes are required. The computational advantage of the reduced order model is clear from the results presented.
publisherThe American Society of Mechanical Engineers (ASME)
titleReduced Order Model Analysis for Two-Dimensional Molecular Dynamic Chain Structure Attached to an Atomic Force Microscope
typeJournal Paper
journal volume126
journal issue3
journal titleJournal of Dynamic Systems, Measurement, and Control
identifier doi10.1115/1.1789969
journal fristpage531
journal lastpage546
identifier eissn1528-9028
keywordsAtomic force microscopy
keywordsEquilibrium (Physics)
keywordsChain
keywordsDynamic response
keywordsEquations
keywordsFrequency
keywordsForce
keywordsMolecular dynamics
keywordsStiffness AND Eigenvalues
treeJournal of Dynamic Systems, Measurement, and Control:;2004:;volume( 126 ):;issue: 003
contenttypeFulltext


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