Search NASA⌕ Search

SEARCH · Search NASA

Results for “three terminal”

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.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 577 records · Page 32
All sourcesNASA NTRSDOE OSTI
DOE OSTI2019

Ligand‐Based Control of Single‐Site vs. Multi‐Site Reactivity by a Trichromium Cluster

Abstract The trichromium cluster ( tbs L)Cr 3 (thf) ([ tbs L] 6− =[1,3,5‐C 6 H 9 (NC 6 H 4 ‐ o ‐NSi t BuMe 2 ) 3 ] 6− ) exhibits steric‐ and solvation‐controlled reactivity with organic azides to form three distinct products: reaction of ( tbs L)Cr 3 (thf) with benzyl azide forms a symmetrized bridging imido complex ( tbs L)Cr 3 ( μ 3 ‐NBn); reaction with mesityl azide in benzene affords a terminally bound imido complex ( tbs L)Cr 3 ( μ 1 ‐NMes); whereas the reaction with mesityl azide in THF leads to terminal N‐atom excision from the azide to yield the nitride complex ( tbs L)Cr 3 ( μ 3 ‐N). The reactivity of this complex demonstrates the ability of the cluster‐templating ligand to produce a well‐defined polynuclear transition metal cluster that can access distinct single‐site and cooperative reactivity controlled by either substrate steric demands or reaction media.

Bartholomew, Amymarie K.↗
DOE OSTI2019

Ligand-Based Control of Single-Site vs. Multi-Site Reactivity by a Trichromium Cluster

The trichromium cluster ( tbs L)Cr 3 (thf) ([ tbs L] 6– =[1,3,5-C 6 H 9 (NC 6 H 4 - o -NSi t BuMe 2 ) 3 ] 6– ) exhibits steric- and solvation-controlled reactivity with organic azides to form three distinct products: reaction of ( tbs L)Cr 3 (thf) with benzyl azide forms a symmetrized bridging imido complex ( tbs L)Cr 3 ( μ 3 -NBn); reaction with mesityl azide in benzene affords a terminally bound imido complex ( tbs L)Cr 3 ( μ 1 -NMes); whereas the reaction with mesityl azide in THF leads to terminal N-atom excision from the azide to yield the nitride complex ( tbs L)Cr 3 ( μ 3 -N). We report the reactivity of this complex demonstrates the ability of the cluster-templating ligand to produce a well-defined polynuclear transition metal cluster that can access distinct single-site and cooperative reactivity controlled by either substrate steric demands or reaction media.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2017

Structure-activity relationships of ω-Agatoxin IVA in lipid membranes

To analyze structural features of ω-Aga IVA, a gating modifier toxin from spider venom, we here investigated the NMR solution structure of ω-Aga IVA within DPC micelles. Under those conditions, the Cys-rich central region of ω-Aga IVA still retains the inhibitor Cys knot motif with three short antiparallel β-strands seen in water. However, {sup 15}N HSQC spectra of ω-Aga IVA within micelles revealed that there are radical changes to the toxin's C-terminal tail and several loops upon binding to micelles. The C-terminal tail of ω-Aga IVA appears to assume a β-turn like conformation within micelles, though it is disordered in water. Whole-cell patch clamp studies with several ω-Aga IVA analogs indicate that both the hydrophobic C-terminal tail and an Arg patch in the core region of ω-Aga IVA are critical for Cav2.1 blockade. These results suggest that the membrane environment stabilizes the structure of the toxin, enabling it to act in a manner similar to other gating modifier toxins, though its mode of interaction with the membrane and the channel is unique. - Highlights: • The NMR structure of ω-Aga IVA in DPC micelles is determined. • ω-Aga IVA stabilized its C-terminal tail with a β-turn structure within micelles. • Both the C-terminal tail and Arg patch play a crucial role for blocking Cav2.1.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2021

Effects of pH on an IDP conformational ensemble explored by molecular dynamics simulation

The conformational ensemble of intrinsically disordered proteins, such as α-synuclein, are responsible for their function and malfunction. Misfolding of α-synuclein can lead to neurodegenerative diseases, and the ability to study their conformations and those of other intrinsically disordered proteins under varying physiological conditions can be crucial to understanding and preventing pathologies. In contrast to well-folded peptides, a consensus feature of IDPs is their low hydropathy and high charge, which makes their conformations sensitive to pH perturbation. We examine a prominent member of this subset of IDPs, α-synuclein, using a divide-and-conquer scheme that provides enhanced sampling of IDP structural ensembles. We constructed conformational ensembles of α-synuclein under neutral (pH ~ 7) and low (pH ~ 3) pH conditions and compared our results with available information obtained from smFRET, SAXS, and NMR studies. Specifically, α-synuclein has been found to in a more compact state at low pH conditions and the structural changes observed are consistent with those from experiments. We also characterize the conformational and dynamic differences between these ensembles and discussed the implication on promoting pathogenic fibril formation. We find that under low pH conditions, neutralization of negatively charged residues leads to compaction of the C-terminal portion of α-synuclein while internal reorganization allows α-synuclein to maintain its overall end-to-end distance. Here, we also observe different levels of intra-protein interaction between three regions of α-synuclein at varying pH and a shift towards more hydrophilic interactions with decreasing pH.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2018

The Structure of the Bifunctional Everninomicin Biosynthetic Enzyme EvdMO1 Suggests Independent Activity of the Fused Methyltransferase-Oxidase Domains

Members of the orthosomycin family of natural products are decorated polysaccharides with potent antibiotic activity and complex biosynthetic pathways. Here, the defining feature of the orthosomycins is an orthoester linkage between carbohydrate moieties that is necessary for antibiotic activity and is likely formed by a family of conserved oxygenases. Everninomicins are octasaccharide orthosomycins produced by Micromonospora carbonacea that have two orthoester linkages and a methylenedioxy bridge, three features whose formation logically requires oxidative chemistry. Correspondingly, the evd gene cluster encoding everninomicin D encodes two monofunctional nonheme iron, α-ketoglutarate-dependent oxygenases and one bifunctional enzyme with an N-terminal methyltransferase domain and a C-terminal oxygenase domain. To investigate whether the activities of these domains are linked in the bifunctional enzyme EvdMO1, we determined the structure of the N-terminal methyltransferase domain to 1.1 Å and that of the full-length protein to 3.35 Å resolution. Both domains of EvdMO1 adopt the canonical folds of their respective superfamilies and are connected by a short linker. Each domain’s active site is oriented such that it faces away from the other domain, and there is no evidence of a channel connecting the two. Our results support EvdMO1 working as a bifunctional enzyme with independent catalytic activities.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2023

Copper Reductase Activity and Free Radical Chemistry by Cataract-Associated Human Lens γ-Crystallins

Cataracts are caused by high-molecular weight aggregates of human eye lens proteins that scatter light, causing lens opacity. Metal ions have emerged as important potential players in the etiology of cataract disease, as human lens γ-crystallins are susceptible to metal-induced aggregation. Here, the interaction of Cu 2+ ions with γD-, γC-, and γS- crystallins, the three most abundant γ-crystallins in the lens, has been evaluated. Cu 2+ ions induced non-amyloid aggregation in all three proteins. Solution turbidimetry, SDS-PAGE, circular dichroism and differential scanning calorimetry showed that the mechanism for Cu-induced aggregation involves: i) loss of beta-sheet structure in the N-terminal domain; ii) decreased thermal and kinetic stability; iii) formation of metal-bridged species; and iv) formation of disulfide-bridged dimers. Electron paramagnetic resonance (EPR) revealed two distinct Cu 2+ binding sites in each protein. Spin quantitation demonstrated reduction of γ-crystallin-bound Cu 2+ ions to Cu + under aerobic conditions, while X-ray absorption spectroscopy (XAS) confirmed the presence of linear or trigonal Cu + binding sites in γ-crystallins. Our EPR and XAS studies revealed that γ-crystallins’ Cu 2+ reductase activity yields a protein-based free radical that is likely a Tyr-based species in human γD-crystallin. This unique free radical chemistry carried out by distinct redox-active Cu sites in human lens γ-crystallins likely contributes to the mechanism of copper-induced aggregation. Finally, in the context of an aging human lens, γ-crystallins could be acting, not only as structural proteins, but also as key players for metal and redox homeostasis.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2015

A Preliminary Study of Building a Transmission Overlay for Regional US Power Grid

Many European countries have taken steps toward a Supergrid in order to transmit large amount of intermittent and remote renewable energy over long distance to load centers. In the US, as the expected increase in renewable generation and electricity demand, similar problem arises. A potential solution is to upgrade the transmission system at a higher voltage by constructing a new overlay grid. This paper will first address basic requirements for such an overlay grid. Potential transmission technologies will also be discussed. A multi-terminal VSC HVDC model is developed in DSATools to implement the overlay grid and a test case on a regional NPCC system will be simulated. Another test system of entire US power grid, with three different interconnections tied together using back-to-back HVDC, is also introduced in this paper. Building an overlay system on top of this test case is ongoing, and will be discussed in future work.

Lei, Yin↗
DOE OSTI2012

Structural Features and Chaperone Activity of the NudC Protein Family

The NudC family consists of four conserved proteins with representatives in all eukaryotes. The archetypal nudC gene from Aspergillus nidulans is a member of the nud gene family that is involved in the maintenance of nuclear migration. This family also includes nudF, whose human orthologue, Lis1, codes for a protein essential for brain cortex development. Three paralogues of NudC are known in vertebrates: NudC, NudC-like (NudCL), and NudC-like 2 (NudCL2). The fourth distantly related member of the family, CML66, contains a NudC-like domain. The three principal NudC proteins have no catalytic activity but appear to play as yet poorly defined roles in proliferating and dividing cells. We present crystallographic and NMR studies of the human NudC protein and discuss the results in the context of structures recently deposited by structural genomics centers (i.e., NudCL and mouse NudCL2). All proteins share the same core CS domain characteristic of proteins acting either as cochaperones of Hsp90 or as independent small heat shock proteins. However, while NudC and NudCL dimerize via an N-terminally located coiled coil, the smaller NudCL2 lacks this motif and instead dimerizes as a result of unique domain swapping. We show that NudC and NudCL, but not NudCL2, inhibit the aggregation of several target proteins, consistent with an Hsp90-independent heat shock protein function. Importantly, and in contrast to several previous reports, none of the three proteins is able to form binary complexes with Lis1. The availability of structural information will be of help in further studies on the cellular functions of the NudC family.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2010

Recognition of the amber UAG stop codon by release factor RF1

We report the crystal structure of a termination complex containing release factor RF1 bound to the 70S ribosome in response to an amber (UAG) codon at 3.6-{angstrom} resolution. The amber codon is recognized in the 30S subunit-decoding centre directly by conserved elements of domain 2 of RF1, including T186 of the PVT motif. Together with earlier structures, the mechanisms of recognition of all three stop codons by release factors RF1 and RF2 can now be described. Our structure confirms that the backbone amide of Q230 of the universally conserved GGQ motif is positioned to contribute directly to the catalysis of the peptidyl-tRNA hydrolysis reaction through stabilization of the leaving group and/or transition state. We also observe synthetic-negative interactions between mutations in the switch loop of RF1 and in helix 69 of 23S rRNA, revealing that these structural features interact functionally in the termination process. These findings are consistent with our proposal that structural rearrangements of RF1 and RF2 are critical to accurate translation termination.

36 MATERIALS SCIENCE↗
DOE OSTI2012

Structural characterization of human Uch37

Uch37 is a deubiquitylating enzyme (DUB) that is functionally linked with multiple protein complexes and signal transduction pathways. Uch37 associates with the 26S proteasome through Rpn13 where it serves to remove distal ubiquitin moeities from polyubiquitylated proteins. Uch37's proteasome associated activity was shown to liberate proteins from destruction. However, Uch37 may also specifically facilitate the destruction of inducible nitric oxide synthase and I{kappa}B-{alpha} at the proteasome. Wicks et al. established Uch37's potential to modulate the transforming growth factor-{beta}(TGF-{beta}) signaling cascade, through tis interaction with SMAD7. Yao et al. demonstrated that Uch37 also associates with the Ino80 chromatin-remodeling complex (Ino80 complex), which is involved in DNA repair and transcriptional regulation. Uch37's importance in metazoan development was underscored recently as Uch37 knockouts in mice result in prenatal lethality, where mutant embryos had severe defects in brain development. Protein ubiquitylation is an ATP-dependent post-translational modification that serves to signal a wide variety of cellular processes in eukaryotes. A protein cascade, generally comprising three enzymes, functions to activate, transport and specifically transfer ubiquitin to the targeted protein, culminating in an isopeptide linkage between the {epsilon}-amino group of a target protein's lysysl residue and the ubiquitin's terminal carboxylate. Monoubiquitination plays an important role in histone regulation, endocytosis, and viral budding. Further processing of the target protein may be accomplished by ubiquitylation of the protein on a different lysine, or through the formation of polyubiquitin chains, where the best-characterized outcome is destruction of the polyubiquitin-labeled protein in the proteasome. DUBs catalyze the removal of ubiquitin from proteins. This activity serves to reverse the effects of ubiquitination, permit ubiquitin recycling, or liberate free ubiquitin after translation. Uch37, is a cysteine protease from the ubiquitin C-terminal hydrolase (UCH) family. The catalytic domain of UCH enzymes has a central, six-stranded, antiparallel {beta}-sheet that is flanked on each side by {alpha}-helices. Like picornain 3C, UCH family proteins contain a catalytic triad comprising the side chains of cysteine, histidine, and aspartate. in picornain 3C, the aspartate's carboxylate side chain acts to position histidine's imidazole group for general base catalysis, which activates cysteine for nucleophilic attack. UCH enzymes also contain a glutamine, which may serve to stabilize the tetrahedral transition state. The UCH family can be divided into two distinct groups, that is, enzymes solely composed of the globular UCH fold, or enzymes comprising the UCH domain and a C-terminal extension. The latter group can be subdivided based on the composition of the C-terminal extension. Uch37 carries a C-terminal extension. Until now, the structure of a full-length UCH from this structural class has not been reported.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2018

The structures of penicillin-binding protein 4 (PBP4) and PBP5 from Enterococci provide structural insights into β-lactam resistance

The final steps of cell-wall biosynthesis in bacteria are carried out by penicillin-binding proteins (PBPs), whose transpeptidase domains form the cross-links in peptidoglycan chains that define the bacterial cell wall. These enzymes are the targets of β-lactam antibiotics, as their inhibition reduces the structural integrity of the cell wall. Bacterial resistance to antibiotics is a rapidly growing concern; however, the structural underpinnings of PBP-derived antibiotic resistance are poorly understood. PBP4 and PBP5 are low-affinity, class B transpeptidases that confer antibiotic resistance to Enterococcus faecalis and Enterococcus faecium, respectively. We report the crystal structures of PBP4 (1.8 Å) and PBP5 (2.7 Å) in their apo and acyl-enzyme complexes with the β-lactams benzylpenicillin, imipenem, and ceftaroline. We found that, although these three β-lactams adopt geometries similar to those observed in other class B PBP structures, there are small, but significant, differences that likely decrease antibiotic efficacy. Further, we also discovered that the N-terminal domain extensions in this class of PBPs undergo large rigid-body rotations without impacting the structure of the catalytic transpeptidase domain. Together, our findings are defining the subtle functional and structural differences in the Enterococcus PBPs that allow them to support transpeptidase activity while also conferring bacterial resistance to antibiotics that function as substrate mimics.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2016

Crystal structure of the fluorescent protein from Dendronephthya sp. in both green and photoconverted red forms

The fluorescent protein from Dendronephthya sp. (DendFP) is a member of the Kaede-like group of photoconvertible fluorescent proteins with a His62-Tyr63-Gly64 chromophore-forming sequence. Upon irradiation with UV and blue light, the fluorescence of DendFP irreversibly changes from green (506 nm) to red (578 nm). The photoconversion is accompanied by cleavage of the peptide backbone at the C α —N bond of His62 and the formation of a terminal carboxamide group at the preceding Leu61. The resulting double C α =C β bond in His62 extends the conjugation of the chromophore π system to include imidazole, providing the red fluorescence. Here, the three-dimensional structures of native green and photoconverted red forms of DendFP determined at 1.81 and 2.14 Å resolution, respectively, are reported. This is the first structure of photoconverted red DendFP to be reported to date. The structure-based mutagenesis of DendFP revealed an important role of positions 142 and 193: replacement of the original Ser142 and His193 caused a moderate red shift in the fluorescence and a considerable increase in the photoconversion rate. It was demonstrated that hydrogen bonding of the chromophore to the Gln116 and Ser105 cluster is crucial for variation of the photoconversion rate. The single replacement Gln116Asn disrupts the hydrogen bonding of Gln116 to the chromophore, resulting in a 30-fold decrease in the photoconversion rate, which was partially restored by a further Ser105Asn replacement.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2015

AGR 3/4 Irradiation Test Final As Run Report

Several fuel and material irradiation experiments have been planned for the Idaho National Laboratory Advanced Reactor Technologies Technology Development Office Advanced Gas Reactor Fuel Development and Qualification Program (referred to as the INL ART TDO/AGR fuel program hereafter), which supports the development and qualification of tristructural-isotropic (TRISO) coated particle fuel for use in HTGRs. The goals of these experiments are to provide irradiation performance data to support fuel process development, qualify fuel for normal operating conditions, support development and validation of fuel performance and fission product transport models and codes, and provide irradiated fuel and materials for post irradiation examination and safety testing (INL 05/2015). AGR-3/4 combined the third and fourth in this series of planned experiments to test TRISO coated low enriched uranium (LEU) oxycarbide fuel. This combined experiment was intended to support the refinement of fission product transport models and to assess the effects of sweep gas impurities on fuel performance and fission product transport by irradiating designed-to-fail fuel particles and by measuring subsequent fission metal transport in fuel-compact matrix material and fuel-element graphite. The AGR 3/4 fuel test was successful in irradiating the fuel compacts to the burnup and fast fluence target ranges, considering the experiment was terminated short of its initial 400 EFPD target (Collin 2015). Out of the 48 AGR-3/4 compacts, 42 achieved the specified burnup of at least 6% fissions per initial heavy-metal atom (FIMA). Three capsules had a maximum fuel compact average burnup < 10% FIMA, one more than originally specified, and the maximum fuel compact average burnup was <19% FIMA for the remaining capsules, as specified. Fast neutron fluence fell in the expected range of 1.0 to 5.5×1025 n/m2 (E >0.18 MeV) for all compacts. In addition, the AGR-3/4 experiment was globally successful in keeping the temperature in the twelve capsules relatively flat in a range of temperatures suitable for the measurement of fission product diffusion in compact matrix and structural graphite materials.

11 NUCLEAR FUEL CYCLE AND FUEL MATERIALS↗
DOE OSTI2016

AGR 3/4 Irradiation Test Final As Run Report, Revision 1

Several fuel and material irradiation experiments have been planned for the Idaho National Laboratory Advanced Reactor Technologies Technology Development Office Advanced Gas Reactor Fuel Development and Qualification Program (referred to as the INL ART TDO/AGR fuel program hereafter), which supports the development and qualification of tristructural-isotropic (TRISO) coated particle fuel for use in HTGRs. The goals of these experiments are to provide irradiation performance data to support fuel process development, qualify fuel for normal operating conditions, support development and validation of fuel performance and fission product transport models and codes, and provide irradiated fuel and materials for post irradiation examination and safety testing (INL 05/2015). AGR-3/4 combined the third and fourth in this series of planned experiments to test TRISO coated low enriched uranium (LEU) oxycarbide fuel. This combined experiment was intended to support the refinement of fission product transport models and to assess the effects of sweep gas impurities on fuel performance and fission product transport by irradiating designed-to-fail fuel particles and by measuring subsequent fission metal transport in fuel-compact matrix material and fuel-element graphite. The AGR 3/4 fuel test was successful in irradiating the fuel compacts to the burnup and fast fluence target ranges, considering the experiment was terminated short of its initial 400 EFPD target (Collin 2015). Out of the 48 AGR-3/4 compacts, 42 achieved the specified burnup of at least 6% fissions per initial heavy-metal atom (FIMA). Three capsules had a maximum fuel compact average burnup < 10% FIMA, one more than originally specified, and the maximum fuel compact average burnup was <19% FIMA for the remaining capsules, as specified. Fast neutron fluence fell in the expected range of 1.0 to 5.5 × 10 25 n/m 2 (E >0.18 MeV) for all compacts. In addition, the AGR-3/4 experiment was globally successful in keeping the temperature in the twelve capsules relatively flat in a range of temperatures suitable for the measurement of fission product diffusion in compact matrix and structural graphite materials.

11 NUCLEAR FUEL CYCLE AND FUEL MATERIALS↗
DOE OSTI2012

Getting Beyond Yucca Mountain - 12305

The U.S. Department of Energy has terminated the Yucca Mountain repository project. The U.S. Nuclear Regulatory Commission has indefinitely suspended the Yucca Mountain licensing proceeding. The presidentially-appointed Blue Ribbon Commission (BRC) on America's Nuclear Future is preparing a report, due in January 2012, to the Secretary of Energy on recommendations for a new national nuclear waste management and disposal program. The BRC Draft Report published in July 2011 provides a compelling critique of the past three decades failed efforts in the United States to site storage and disposal facilities for spent nuclear fuel (SNF) and high-level radioactive waste (HLW). However, the BRC Draft Report fails to provide detailed guidance on how to implement an alternative, successful approach to facility site selection. The comments submitted to the BRC by the State of Nevada Agency for Nuclear Projects provide useful details on how the US national nuclear waste program can get beyond the failed Yucca Mountain repository project. A detailed siting process, consisting of legislative elements, procedural elements, and 'rules' for volunteer sites, could meet the objectives of the BRC and the Western Governors Association (WGA), while promoting and protecting the interests of potential host states. The recent termination of the proposed Yucca Mountain repository provides both an opportunity and a need to re-examine the United States' nuclear waste management program. The BRC Draft Report published in July 2011 provides a compelling critique of the past three decades failed efforts in the United States to site storage and disposal facilities for SNF and HLW. It is anticipated that the BRC Final report in January 2012 will recommend a new general course of action, but there will likely continue to be a need for detailed guidance on how to implement an alternative, successful approach to facility site selection. Getting the nation's nuclear waste program back on track requires, among other things, new principles for siting-principles based on partnership between the federal implementing agency and prospective host states. These principles apply to the task of developing an integrated waste management strategy, to interactions between the federal government and prospective host states for consolidated storage and disposal facilities, and to the logistically and politically complicated task of transportation system design. Lessons from the past 25 years, in combination with fundamental parameters of the nuclear waste management task in the US, suggest new principles for partnership outlined in this paper. These principles will work better if well-grounded and firm guidelines are set out beforehand and if the challenge of maintaining competence, transparency and integrity in the new organization is treated as a problem to be addressed rather than a result to be expected. (authors)

12 MANAGEMENT OF RADIOACTIVE AND NON-RADIOACTIVE W↗
DOE OSTI2012

Single Molecule Kinetics of ENTH Binding to Lipid Membranes

Transient recruitment of proteins to membranes is a fundamental mechanism by which the cell exerts spatial and temporal control over proteins’ localization and interactions. Thus, the specificity and the kinetics of peripheral proteins’ membrane residence are an attribute of their function. In this article, we describe the membrane interactions of the interfacial epsin N-terminal homology (ENTH) domain with its target lipid phosphatidylinositol (4,5)-bisphosphate (PtdIns(4,5)P 2 ). The direct visualization and quantification of interactions of single ENTH molecules with supported lipid bilayers is achieved using total internal reflection fluorescence microscopy (TIRFM) with a time resolution of 13 ms. This enables the recording of the kinetic behavior of ENTH interacting with membranes with physiologically relevant concentrations of PtdIns(4,5)P 2 despite the low effective binding affinity. Subsequent single fluorophore tracking permits us to build up distributions of residence times and to measure ENTH dissociation rates as a function of membrane composition. In addition, due to the high time resolution, we are able to resolve details of the motion of ENTH associated with a simple, homogeneous membrane. In this case ENTH’s diffusive transport appears to be the result of at least three different diffusion processes.

membrane-protein interactions↗
DOE OSTI2015

Regional and Local Geothermal Potential Evaluation: Examples from the Great Basin, USA, Iceland and East Africa

In both tectonically and magmatically mediated geothermal systems, geologic structures play a crucial role in focusing geothermal fluid circulation in the upper crust. In a variety of geothermal provinces worldwide, normal and strike-slip faults, caldera related faults, as well as fractures and fissures related to dikes and other magmatic intrusions generate the fracture permeability utilized for geothermal circulation. Localities where the above structures intersect and interact are characterized by the most robust generation and maintenance of fracture permeability, and therefore are the most favorable conduits for geothermal circulation. We present an evaluation of the structural geometries that tend to generate high density faulting and fracturing and an evaluation of the orientations of those structures with respect to the ambient stress conditions in three regions of high geothermal potential; The Great Basin, USA, Iceland, and east Africa. These analyses provide first-order constraints on areas that have favorable conditions for permeability and where future exploration for geothermal resources could be focused. In the Great Basin, USA, fault step-overs, fault terminations and accommodation zones are among the most common structural settings of known geothermal activity. Analysis of the geometry of these structures with respect to the ambient stress conditions reveals locations where faults associated with these structures are favorably oriented for enhanced fracture permeability. In magmatically active extensional provinces, like Iceland and east Africa, heat associated with shallow magmatic intrusions beneath volcanic centers drives geothermal circulation in near-surface fracture permeability conduits. Accentuated fault and fracture density and fracture permeability is generated by both axially oriented faults and fractures associated with axial rift zones and radially oriented structures near volcanic centers. Although heat from magmatic intrusion is most robust at volcanic centers, a high density of young intrusions may actually result in decreased permeability through closing of fracture networks. The locations of these three types of features; axial faults and fractures, radial structures, and young magmatic intrusions, all play a critical role in determining the most favorable locations for fracture permeability and fluid flow in magmatic geothermal systems. Within and around the margins of volcanic centers, where radial structures associated with volcanic centers interact and intersect with axially oriented structures associated with axial extension are the most favorable locations for fracture permeability and geothermal fluid circulation in magmatic extensional geothermal systems.

15 GEOTHERMAL ENERGY↗
DOE OSTI2012

A New Structural Form in the SAM/Metal-Dependent O;#8209;Methyltransferase Family: MycE from the Mycinamicin Biosynthetic Pathway

O-linked methylation of sugar substituents is a common modification in the biosynthesis of many natural products and is catalyzed by multiple families of S-adenosyl-l-methionine (SAM or AdoMet)-dependent methyltransferases (MTs). Mycinamicins, potent antibiotics from Micromonospora griseorubida, can be methylated at two positions on a 6-deoxyallose substituent. The first methylation is catalyzed by MycE, a SAM- and metal-dependent MT. Crystal structures were determined for MycE bound to the product S-adenosyl-l-homocysteine (AdoHcy) and magnesium, both with and without the natural substrate mycinamicin VI. This represents the first structure of a natural product sugar MT in complex with its natural substrate. MycE is a tetramer of a two-domain polypeptide, comprising a C-terminal catalytic MT domain and an N-terminal auxiliary domain, which is important for quaternary assembly and for substrate binding. The symmetric MycE tetramer has a novel MT organization in which each of the four active sites is formed at the junction of three monomers within the tetramer. The active-site structure supports a mechanism in which a conserved histidine acts as a general base, and the metal ion helps to position the methyl acceptor and to stabilize a hydroxylate intermediate. A conserved tyrosine is suggested to support activity through interactions with the transferred methyl group from the SAM methyl donor. The structure of the free enzyme reveals a dramatic order-disorder transition in the active site relative to the S-adenosyl-L-homocysteine complexes, suggesting a mechanism for product/substrate exchange through concerted movement of five loops and the polypeptide C-terminus.

60 APPLIED LIFE SCIENCES↗