Aerodynamic Analyses and Database Development for Ares I Vehicle First Stage Separation

This paper presents the aerodynamic analysis and database development for first stage separation of Ares I A106 crew launch vehicle configuration. Separate 6-DOF databases were created for the first stage and upper stage and each database consists of three components: (a) isolated or freestream coefficients, (b) power-off proximity increments, and (c) power-on proximity increments. The isolated and power-off incremental databases were developed using data from 1% scaled model tests in AEDC VKF Tunnel A. The power-on proximity increments were developed using OVERFLOW CFD solutions. The database also includes incremental coefficients for one BDM and one USM failure scenarios

Role of Secondary Motifs in Fast Folding Polymers: A Dynamical Variational Principle

A fascinating and open question challenging biochemistry, physics and even geometry is the presence of highly regular motifs such as alpha-helices in the folded state of biopolymers and proteins. Stimulating explanations ranging from chemical propensity to simple geometrical reasoning have been invoked to rationalize the existence of such secondary structures. We formulate a dynamical variational principle for selection in conformation space based on the requirement that the backbone of the native state of biologically viable polymers be rapidly accessible from the denatured state. The variational principle is shown to result in the emergence of helical order in compact structures.Comment: 4 pages, RevTex, 4 eps figure

Protein structures and optimal folding emerging from a geometrical variational principle

Novel numerical techniques, validated by an analysis of barnase and chymotrypsin inhibitor, are used to elucidate the paramount role played by the geometry of the protein backbone in steering the folding to the correct native state. It is found that, irrespective of the sequence, the native state of a protein has exceedingly large number of conformations with a given amount of structural overlap compared to other compact artificial backbones; moreover the conformational entropies of unrelated proteins of the same length are nearly equal at any given stage of folding. These results are suggestive of an extremality principle underlying protein evolution, which, in turn, is shown to be associated with the emergence of secondary structures.Comment: Revtex, 5 pages, 5 postscript figure

Digital Signal Processing

Contains an introduction and reports on fifteen research projects.National Science Foundation FellowshipU.S. Navy - Office of Naval Research (Contract N00014-81-K-0742)National Science Foundation (Grant ECS 84-07285)Sanders Associates, Inc.U.S. Air Force - Office of Scientific Research (Contract F19628-85-K-0028)AT&T Bell Laboratories Doctoral Support ProgramCanada, Bell Northern Research ScholarshipCanada, Fonds pour la Formation de Chercheurs et /'Aide a la Recherche Postgraduate FellowshipCanada, Natural Science and Engineering Research Council Postgraduate FellowshipAmoco Foundation FellowshipFannie and John Hertz Foundation Fellowshi

Digital Signal Processing

Contains table of contents for Part III, table of contents for Section 1, an introduction and reports on seventeen research projects.National Science Foundation FellowshipNational Science Foundation (Grant ECS 84-07285)National Science Foundation (Grant MIP 87-14969)U.S. Navy - Office of Naval Research (Contract N00014-81-K-0742)Scholarship from the Federative Republic of BrazilU.S. Air Force - Electronic Systems Division (Contract F19628-85-K-0028)AT&T Bell Laboratories Doctoral Support ProgramCanada, Bell Northern Research ScholarshipCanada, Fonds pour la Formation de Chercheurs et I'Aide a la Recherche Postgraduate FellowshipSanders Associates, Inc.OKI Semiconductor, Inc.Tel Aviv University, Department of Electronic SystemsU.S. Navy - Office of Naval Research (Contract N00014-85-K-0272)Natural Sciences and Engineering Research Council of Canada, Science and Engineering Scholarshi

Use of machine learning algorithms to classify binary protein sequences as highly-designable or poorly-designable

<p>Abstract</p> <p>Background</p> <p>By using a standard Support Vector Machine (SVM) with a Sequential Minimal Optimization (SMO) method of training, Naïve Bayes and other machine learning algorithms we are able to distinguish between two classes of protein sequences: those folding to highly-designable conformations, or those folding to poorly- or non-designable conformations.</p> <p>Results</p> <p>First, we generate all possible compact lattice conformations for the specified shape (a hexagon or a triangle) on the 2D triangular lattice. Then we generate all possible binary hydrophobic/polar (H/P) sequences and by using a specified energy function, thread them through all of these compact conformations. If for a given sequence the lowest energy is obtained for a particular lattice conformation we assume that this sequence folds to that conformation. Highly-designable conformations have many H/P sequences folding to them, while poorly-designable conformations have few or no H/P sequences. We classify sequences as folding to either highly – or poorly-designable conformations. We have randomly selected subsets of the sequences belonging to highly-designable and poorly-designable conformations and used them to train several different standard machine learning algorithms.</p> <p>Conclusion</p> <p>By using these machine learning algorithms with ten-fold cross-validation we are able to classify the two classes of sequences with high accuracy – in some cases exceeding 95%.</p

Digital Signal Processing

Contains an introduction and reports on twenty research projects.National Science Foundation (Grant ECS 84-07285)U.S. Navy - Office of Naval Research (Contract N00014-81-K-0742)National Science Foundation FellowshipSanders Associates, Inc.U.S. Air Force - Office of Scientific Research (Contract F19628-85-K-0028)Canada, Bell Northern Research ScholarshipCanada, Fonds pour la Formation de Chercheurs et l'Aide a la Recherche Postgraduate FellowshipCanada, Natural Science and Engineering Research Council Postgraduate FellowshipU.S. Navy - Office of Naval Research (Contract N00014-81-K-0472)Fanny and John Hertz Foundation FellowshipCenter for Advanced Television StudiesAmoco Foundation FellowshipU.S. Air Force - Office of Scientific Research (Contract F19628-85-K-0028

Signal Processing Research Program

Contains table of contents for Part III, table of contents for Section 1, an introduction and reports on fourteen research projects.Charles S. Draper Laboratory Contract DL-H-404158U.S. Navy - Office of Naval Research Grant N00014-89-J-1489National Science Foundation Grant MIP 87-14969Battelle LaboratoriesTel-Aviv University, Department of Electronic SystemsU.S. Army Research Office Contract DAAL03-86-D-0001The Federative Republic of Brazil ScholarshipSanders Associates, Inc.Bell Northern Research, Ltd.Amoco Foundation FellowshipGeneral Electric FellowshipNational Science Foundation FellowshipU.S. Air Force - Office of Scientific Research FellowshipU.S. Navy - Office of Naval Research Grant N00014-85-K-0272Natural Science and Engineering Research Council of Canada - Science and Technology Scholarshi