355 research outputs found
A Fast and Accurate Process Variation-aware Modeling Technique for Resistive Bridge Defects
No full textRecent research has shown that tests generated without taking process variation into account may lead to loss of test quality. At present there is no efficient device-level modeling technique that models the effect of process variation on resistive bridge defects. This paper presents a fast and accurate technique to achieve this, including modeling the effect of voltage and temperature variation using BSIM4 transistor model. To speedup the computation time and without compromising simulation accuracy (achieved through BSIM4) two efficient voltage approximation algorithms are proposed for calculating logic threshold of driven gates and voltages on bridged lines of a fault-site to calculate bridge critical resistance. Experiments are conducted on a 65-nm gate library (for illustration purposes), and results show that on average the proposed modeling technique is more than 53 times faster and in the worst case, error in bridge critical resistance is 2.64% when compared with HSPICE
Solution and Membrane Bound Conformational Properties of a Peptide from the First Extracellular Loop of the Angiotensin II AT1 Receptor
No full textSolution and Membrane Bound Conformational Properties of a Peptide from the First Extracellular Loop of the Angiotensin II AT1 Receptor
No full textStabilization of a Predicted Turn in a Peptide from the First Extra-cellular Loop of the Angiotensin II AT1 Receptor in Trifluoroethanol and upon Binding to Model Membranes
No full textDepth and Insertion Studies of the Angiotensin II AT1A Receptor Second Intracellular Loop (IL2) in Model Membranes Using Differential Fluorescence Quenching
No full textThe angiotensin II AT1A receptor - A Fluorescence Quenching Study of the Depth of Insertion of the Receptor's SecondIntra-Cellular Loop (IL2) in Model Membranes
No full textCD and Fluorescence Studies of the Angiotensin II AT1A Receptor Second Intracellular Loop in Solution and in the Presence of Model Membranes
No full textTrifluoroethanol and binding to model membranes stabilize a predicted turn in a peptide corresponding to the first extracellular loop of the angiotensin II AT(1A) receptor
No full textHomology modeling of the angiotensin H AT(1A) receptor based oil rhodopsin's crystal structure has assigned the 92-100 (YRWPFGNHL) sequence of the receptor to its first extracellular loop. Solution and membrane-bound conformational properties of a peptide containing this sequence (EL1) were examined by CD, fluorescence, and H-1-NMR. CD spectra in aqueous solution revealed an equilibrium between less organized and folded conformers. NMR spectra indicated the coexistence of trans and cis isomers of the Trp(3)-Pro(4) bond. A positive band at 226 urn in the CD spectra suggested aromatic ring stacking, modulated by EL1's ionization degree. CD spectra showed that trifluoroethanol (TFE), or binding to detergent micelles and phospholipid bilayers, shifted the equilibrium toward conformers with higher secondary structure content. Different media gave rise to spectra suggestive of different beta-turns. Chemical shaft changes in the NMR spectra corroborated the stabilization of different conformations. Thus, environments of lower polarity or binding to interfaces probably favored the formation of hydrogen bonds, stabilizing beta-turns, predicted for this sequence in the whole receptor. Increases in Trp(3) fluorescence intensity and anisotropy, blue shifts of the maximum emission wavelength, and pK changes also evinced the interaction between EL1 and model membranes. Binding was seen to depend on both hydrophobic and electrostatic interactions, as well cis lipid phase packing. Studies with water-soluble and membrane-bound fluorescence quenchers demonstrated that Trp(3) is located close to the water-membrane interface. the results are discussed with regard to possible implications in receptor folding and function. (C) 2002 Wiley Periodicals, Inc. Biopolymers 65: 21-31, 2002.Univ São Paulo, Dept Biochem, Inst Chem, BR-05513970 São Paulo, BrazilNatl Lab Synchrotron Light, Ctr Mol & Struct Biol, Campinas, BrazilUniversidade Federal de São Paulo, Dept Biophys, São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biophys, São Paulo, BrazilWeb of Scienc
Conformational Studies of the second Intracellular Loop of the Angiotensin II AT1A Receptor
No full textSupport Vector Classifiers in scikit-learn: Mathematical Detail, Part II
No full textWe present mathematical detail pertaining to the theory of soft-margin support vector classifiers, designated C-SVC, as used in scikit-learn. We discuss the character of C-SVC, particularly with regard to the penalty term. We construct the primal problem and, thereafter, derive the dual problem. We introduce the notion of nonlinear classifiers and describe the so-called kernel trick. Additionally, we show how the primal problem can be derived from the dual problem. The paper is the second in a series and is intended to be educational in nature.
Tunawasilisha maelezo ya hisabati yanayohusiana na nadharia ya viainishaji vya vekta vya usaidizi wa ukingo laini, iliyoteuliwa C-SVC, kama inavyotumiwa katika kujifunza kwa scikit. Tunajadili tabia ya C-SVC, hasa kuhusu muda wa adhabu. Tunaunda shida ya msingi na, baada ya hapo, tunapata shida mbili. Tunatanguliza wazo la viainishaji visivyo vya mstari na kuelezea kinachojulikana kama hila ya kernel. Zaidi ya hayo, tunaonyesha jinsi shida ya msingi inaweza kupatikana kutoka kwa shida mbili. Karatasi ni ya pili katika mfululizo na inakusudiwa kuwa ya elimu kwa asili.
(The translation into Swahili was provided by Google Translate)
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