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Results for “higher-order assembly”

Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.

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11 records
All sourcesNASA NTRSDOE OSTI
NASA NTRS2003

Membrane-Based Functions in the Origin of Cellular Life

How simple membrane peptides performed such essential proto-cellular functions as transport of ions and organic matter across membranes separating the interior of the cell from the environment, capture and utilization of energy, and transduction of environmental signals, is a key question in protobiological evolution. On the basis of detailed, molecular-level computer simulations we investigate how these peptides insert into membranes, self-assemble into higher-order structures and acquire functions. We have studied the insertion of an a-helical peptide containing leucine (L) and serine (S) of the form (LSLLLSL)S into a model membrane. The transmembrane state is metastable, and approximately 15 kcal/mol is required to insert the peptide into the membrane. Investigations of dimers formed by (LSLLLSL)S and glycophorin A demonstrate how the favorable free energy of helix association can offset the unfavorable free energy of insertion, leading to self- assembly of peptide helices in the membrane. An example of a self-assembled structure is the tetrameric transmembrane pore of the influenza virus M2 protein, which is an efficient and selective voltage-gated proton channel. Our simulations explain the gating mechanism and provide guidelines how to reengineering the channel to act as a simple proton pump. In general, emergence of integral membrane proteins appears to be quite feasible and may be easier to envision than the emergence of water-soluble proteins.

Wilson, Michael A.↗
NASA NTRS2003

Membrane peptides and their role in protobiological evolution

How simple membrane peptides performed such essential protocellular functions as transport of ions and organic matter across membranes separating the interior of the cell from the environment, capture and utilization of energy, and transduction of environmental signals, is a key question in protobiological evolution. On the basis of detailed, molecular-level computer simulations we explain how these peptides fold at water-membrane interfaces, insert into membranes, self-assemble into higher-order structures and acquire functions. We have investigated the interfacial behavior and folding of several peptides built of leucine and glutamine residues and have demonstrated that many of them tend to adopt ordered structures. Further, we have studied the insertion of an alpha-helical peptide containing leucine (L) and serine (S) of the form (LSLLLSL)3 into a model membrane. The transmembrane state is metastable, and approximately 15 kcal mol(-1) is required to insert the peptide into the membrane. Investigations of dimers formed by (LSLLLSL)3 and glycophorin A demonstrate how the favorable free energy of helix association can offset the unfavorable free energy of insertion, leading to self-assembly of peptide helices in the membrane. An example of a self-assembled structure is the tetrameric transmembrane pore of the influenza virus M2 protein, which is an efficient and selective voltage-gated proton channel. Our simulations explain the gating mechanism and provide guidelines how to re-engineer the channel to act as a simple proton pump. In general, emergence of integral membrane proteins appears to be quite feasible and may be easier to envision than the emergence of water-soluble proteins.

Models, Chemical↗
NASA NTRS2005

The Origin and Early Evolution of Membrane Proteins

Membrane proteins mediate functions that are essential to all cells. These functions include transport of ions, nutrients and waste products across cell walls, capture of energy and its transduction into the form usable in chemical reactions, transmission of environmental signals to the interior of the cell, cellular growth and cell volume regulation. In the absence of membrane proteins, ancestors of cell (protocells), would have had only very limited capabilities to communicate with their environment. Thus, it is not surprising that membrane proteins are quite common even in simplest prokaryotic cells. Considering that contemporary membrane channels are large and complex, both structurally and functionally, a question arises how their presumably much simpler ancestors could have emerged, perform functions and diversify in early protobiological evolution. Remarkably, despite their overall complexity, structural motifs in membrane proteins are quite simple, with a-helices being most common. This suggests that these proteins might have evolved from simple building blocks. To explain how these blocks could have organized into functional structures, we performed large-scale, accurate computer simulations of folding peptides at a water-membrane interface, their insertion into the membrane, self-assembly into higher-order structures and function. The results of these simulations, combined with analysis of structural and functional experimental data led to the first integrated view of the origin and early evolution of membrane proteins.

Pohorille, Andrew↗
NASA NTRS2004

Ordered Nanostructures Made Using Chaperonin Polypeptides

A recently invented method of fabricating periodic or otherwise ordered nanostructures involves the use of chaperonin polypeptides. The method is intended to serve as a potentially superior and less expensive alternative to conventional lithographic methods for use in the patterning steps of the fabrication of diverse objects characterized by features of the order of nanometers. Typical examples of such objects include arrays of quantum dots that would serve as the functional building blocks of future advanced electronic and photonic devices. A chaperonin is a double-ring protein structure having a molecular weight of about 60 plus or minus 5 kilodaltons. In nature, chaperonins are ubiquitous, essential, subcellular structures. Each natural chaperonin molecule comprises 14, 16, or 18 protein subunits, arranged as two stacked rings approximately 16 to 18 nm tall by approximately 15 to 17 nm wide, the exact dimensions depending on the biological species in which it originates. The natural role of chaperonins is unknown, but they are believed to aid in the correct folding of other proteins, by enclosing unfolded proteins and preventing nonspecific aggregation during assembly. What makes chaperonins useful for the purpose of the present method is that under the proper conditions, chaperonin rings assemble themselves into higher-order structures. This method exploits such higher-order structures to define nanoscale devices. The higher-order structures are tailored partly by choice of chemical and physical conditions for assembly and partly by using chaperonins that have been mutated. The mutations are made by established biochemical techniques. The assembly of chaperonin polypeptides into such structures as rings, tubes, filaments, and sheets (two-dimensional crystals) can be regulated chemically. Rings, tubes, and filaments of some chaperonin polypeptides can, for example, function as nano vessels if they are able to absorb, retain, protect, and release gases or chemical reagents, including reagents of medical or pharmaceutical interest. Chemical reagents can be bound in, or released from, such structures under suitable controlled conditions. In an example of a contemplated application, a two-dimensional crystal of chaperonin polypeptides would be formed on a surface of an inorganic substrate and used to form a planar array of nanoparticles or quantum dots. Through genetic engineering of the organisms used to manufacture the chaperonins, specific sites on the chaperonin molecules and, thus, on the two-dimensional crystals can be chemically modified to react in a specific manner so as to favor the deposition of the material of the desired nanoparticles or quantum dots. A mutation that introduces a cysteine residue at the desired sites on a chaperonin of Sulfolobus shibatae was used to form planar arrays of gold nanoparticles (see figure).

Trent, Jonathan↗
NASA NTRS1972

A design study for the addition of higher order parametric discrete elements to NASTRAN

The addition of discrete elements to NASTRAN poses significant interface problems with the level 15.1 assembly modules and geometry modules. Potential problems in designing new modules for higher-order parametric discrete elements are reviewed in both areas. An assembly procedure is suggested that separates grid point degrees of freedom on the basis of admissibility. New geometric input data are described that facilitate the definition of surfaces in parametric space.

Stanton, E. L.↗
NASA NTRS2021

The Io GIS Database 1.0: A Proto-Io Planetary Spatial Data Infrastructure

We collected a set of published, higher-order data products of Jupiterʼs volcanic moon Io and assembled them in an ArcGISTM database we are calling the Io GIS Database, version 1.0. The purpose of this database is to collect image, topographic, geologic, and thermal emission data of Io in one geospatially registered location to form the data component of an Io planetary spatial data infrastructure (PSDI). The goals of an Io PSDI are (1) to make higher-order data products more accessible and usable to the broader planetary science community, particularly to new scientists that were not associated with the projects that obtained the data; (2) to enable new scientific studies with the data; and (3) to create a tool to support observation planning for future Io-focused planetary missions. In this paper we describe the motivation behind our project, discuss the data sets acquired for this first version of the database, and demonstrate how they can be used. We conclude with a discussion of how our database relates to other PSDIs, our plans for future updates, and a request for additional Io data sets.

David A Williams↗
NASA NTRS2023

The First Extragalactic Detection of Higher-Order Hydrogen Recombination Lines

The Large Magellanic Cloud (LMC) is the nearest (~50 kpc) star-forming galaxy characterized by a low metallicity (Z~0.3-0.5 Z⨀) similar to galaxies during the early phases of their assembly. As a result, star formation studies in the LMC provide a stepping stone to understanding star formation at earlier epochs of the universe where these processes cannot be directly observed. N113 is one of the most prominent star-forming regions in the LMC hosting one of the most massive giant molecular clouds. N113 is small enough to be imaged in its entirety, but large enough to showcase many important phenomena such as multiple generations of stars, stellar feedback, and different environments. We present our findings from an investigation of the early stages of star formation in the N113 region using the Atacama Large Millimeter/submillimeter Array (ALMA) molecular line data probing a wide density range: 12CO, 13CO, and C18O (2-1), 13CO and C18O (1-0), HCN (1-0), HCO+ (1-0), H13CN (1-0) and (3-2), H13CO+ (1-0) and (3-2), CS (2-1) and (5-4), as well as 1.3 mm and 3 mm continuum. We used the Python package quickclump to identify molecular clumps. We utilized the multiline non-LTE fitting tool based on models from RADEX developed by Finn et al. (2021, ApJ, 917, 106) to construct the CO, HCN, HCO+, and CS temperature and column density, and the H2 density maps of N113. We constructed a catalog of molecular clumps including their physical properties, chemical abundances, sizes, velocities, and velocity dispersions. To establish the evolutionary status of the clumps, their positions were compared with previously identified young stellar objects (YSOs) from the Spitzer/SAGE and Herschel/HERITAGE surveys, as well as water and OH masers. We compared the properties of the clumps in N113 to those in the Galaxy and other regions in the LMC to assess the impact of the environment (e.g., metallicity, stellar feedback) on the star formation process.

Marta M Sewilo↗
NASA NTRS2001

Simulation of Peptides at Aqueous Interfaces

Behavior of peptides at water-membrane interfaces is of great interest in studies on cellular transport and signaling, membrane fusion, and the action of toxins and antibiotics. Many peptides, which exist in water only as random coils, can form sequence-dependent, ordered structures at aqueous interfaces, incorporate into membranes and self-assembly into functional units, such as simple ion channels. Multi -nanosecond molecular dynamics simulations have been carried out to study the mechanism and energetics of interfacial folding of both non-polar and amphiphilic peptides, their insertion into membranes and association into higher-order structures. The simulations indicate that peptides fold non-sequentially, often through a series of amphiphilic intermediates. They further incorporate into the membrane in a preferred direction as folded monomers, and only then aggregate into dimers and, possibly, further into "dimers of dimers".

Pohorille, Andrew↗
NASA NTRS1985

A 3-component laser-Doppler velocimeter data acquisition and reduction system

A laser doppler velocimeter capable of measuring all three components of velocity simultaneously in low-speed flows is described. All the mean velocities, Reynolds stresses, and higher-order products can be evaluated. The approach followed is to split one of the two colors used in a 2-D system, thus creating a third set of beams which is then focused in the flow from an off-axis direction. The third velocity component is computed from the known geometry of the system. The laser optical hardware and the data acquisition electronics are described in detail. In addition, full operating procedures and listings of the software (written in BASIC and ASSEMBLY languages) are also included. Some typical measurements obtained with this system in a vortex/mixing layer interaction are presented and compared directly to those obtained with a cross-wire system.

Rodman, L. C.↗
NASA NTRS1986

A 3-component laser-Doppler velocimeter data acquisition and reduction system

This report describes a laser Doppler velocimeter capable of measuring all three components of velocity simultaneously in low-speed flows. All the mean velocities, Reynolds stresses, and higher-order products can then be evaluated. The approach followed is to split one of the colors used in a 2-D system, thus creating a third set of beams which is then focused in the flow from an off-axis direction. The third velocity component is computed from the known geometry of the system. In this report, the laser optical hardware and the data acquisition electronics are described in detail. In addition, full operating procedures and listings of the software (written in BASIC and assembly languages) are also included. Some typical measurements obtained with this system in a vortex/mixing layer interaction are presented and compared directly to those obtained with a cross-wire system.

Rodman, L. C.↗
NASA NTRS2006

Ka-Band Wide-Bandgap Solid-State Power Amplifier: Prototype Combiner Spurious Mode Suppression and Power Constraints

Results of prototype hardware activities related to a 120-W, 32-GHz (Ka-band) solid-state power amplifier (SSPA) architecture study are presented. Spurious mode suppression and the power-handling capability of a prototype 24-way radial combiner and a prototype 2-way septum binary combiner were investigated. Experimental data indicate that a commercial absorptive filter, designed to pass the circular TE01 mode, effectively suppressed the higher-order modes generated by a narrowband, flower-petal-type mode transducer. However, the same filter was not effective in suppressing higher-order modes generated by the broadband Marie mode transducer that is used in the prototype waveguide radial combiner. Should greater filtering be required by a particular SSPA application, a broadband mode filter that can suppress specifically those higher-order modes that are generated by the Marie transducer will need to be developed. A back-to-back configuration of the prototype radial combiner was tested with drive power up to approximately 50 W. No anomalous behavior was observed. Power measurements of the septum combiner indicate that up to 10-W radio frequency (RF) can be dissipated in the integrated resistive element before a permanent performance shift is observed. Thus, a given adder (a single-stage, 2-way combiner) can safely combine two 20-W sources, and the adder will not be damaged in the event of a source failure. This result is used to calculate the maximum source power that can be safely combined as a function of the number of sources combined and the number of source failures allowed in a multi-stage combiner. The analysis shows that SSPA power >140 W can be generated by power combining 16 sources producing 10 W each. In this configuration, up to three sources could fail with the guarantee that the combiner would not be damaged. Finally, a modified prototype septum combiner design was verified. The improved design reduced the assembly time from over 2 hours to about 15 minutes per adder.

Khan, P.↗