Efficient Estimation of Clamped Step-Thickness Plates FRFs in Industrial Systems

Author(s):  
Yum Ji Chan ◽  
Chung-Yu Tai ◽  
Yuan-You Li
Author(s):  
C. Boulesteix ◽  
C. Colliex ◽  
C. Mory ◽  
B. Pardo ◽  
D. Renard

Contrast mechanisms, which are responsible of the various types of image formation, are generally thickness dependant. In the following, two imaging modes in the 100 kV CTEM are described : they are highly sensitive to thickness variations and can be used for quantitative estimations of step heights.Detailed calculations (1) of the bright-field intensity have been carried out in the 3 (or 2N+l)-beam symmetric case. They show that in given conditions, the two important symmetric Bloch waves interfere most strongly at a critical thickness for which they have equal emergent amplitudes (the more excited wave at the entrance surface is also the more absorbed). The transmitted intensity I for a Nd2O3 specimen has been calculated as a function of thickness t. The capacity of the method to detect a step and measure its height can be more clearly deduced from a plot of dl/Idt as shown in fig. 1.


1967 ◽  
Vol 46 (3) ◽  
pp. 181
Author(s):  
William K. Roots

2020 ◽  
Author(s):  
E. Prabhu Raman ◽  
Thomas J. Paul ◽  
Ryan L. Hayes ◽  
Charles L. Brooks III

<p>Accurate predictions of changes to protein-ligand binding affinity in response to chemical modifications are of utility in small molecule lead optimization. Relative free energy perturbation (FEP) approaches are one of the most widely utilized for this goal, but involve significant computational cost, thus limiting their application to small sets of compounds. Lambda dynamics, also rigorously based on the principles of statistical mechanics, provides a more efficient alternative. In this paper, we describe the development of a workflow to setup, execute, and analyze Multi-Site Lambda Dynamics (MSLD) calculations run on GPUs with CHARMm implemented in BIOVIA Discovery Studio and Pipeline Pilot. The workflow establishes a framework for setting up simulation systems for exploratory screening of modifications to a lead compound, enabling the calculation of relative binding affinities of combinatorial libraries. To validate the workflow, a diverse dataset of congeneric ligands for seven proteins with experimental binding affinity data is examined. A protocol to automatically tailor fit biasing potentials iteratively to flatten the free energy landscape of any MSLD system is developed that enhances sampling and allows for efficient estimation of free energy differences. The protocol is first validated on a large number of ligand subsets that model diverse substituents, which shows accurate and reliable performance. The scalability of the workflow is also tested to screen more than a hundred ligands modeled in a single system, which also resulted in accurate predictions. With a cumulative sampling time of 150ns or less, the method results in average unsigned errors of under 1 kcal/mol in most cases for both small and large combinatorial libraries. For the multi-site systems examined, the method is estimated to be more than an order of magnitude more efficient than contemporary FEP applications. The results thus demonstrate the utility of the presented MSLD workflow to efficiently screen combinatorial libraries and explore chemical space around a lead compound, and thus are of utility in lead optimization.</p>


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