17 results on '"Donald, Bruce"'
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2. Pyroclastic dune bedforms: macroscale structures and lateral variations. Examples from the 2006 pyroclastic currents at Tungurahua (Ecuador).
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Douillet, Guilhem Amin, Bernard, Benjamin, Bouysson, Mélanie, Chaffaut, Quentin, Dingwell, Donald Bruce, Gegg, Lukas, Hoelscher, Inga, Kueppers, Ulrich, Mato, Célia, Ritz, Vanille Ariane, Schlunegger, Fritz, and Witting, Patrick
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SAND dunes ,EXPLOSIVE volcanic eruptions ,WIND speed ,TURBIDITY currents ,GAS flow ,FRICTION velocity - Abstract
Pyroclastic currents are catastrophic flows of gas and particles triggered by explosive volcanic eruptions. For much of their dynamics, they behave as particulate density currents and share similarities with turbidity currents. Pyroclastic currents occasionally deposit dune bedforms with peculiar lamination patterns, from what is thought to represent the dilute low concentration and fluid‐turbulence supported end member of the pyroclastic currents. This article presents a high resolution dataset of sediment plates (lacquer peels) with several closely spaced lateral profiles representing sections through single pyroclastic bedforms from the August 2006 eruption of Tungurahua (Ecuador). Most of the sedimentary features contain backset bedding and preferential stoss‐face deposition. From the ripple scale (a few centimetres) to the largest dune bedform scale (several metres in length), similar patterns of erosive‐based backset beds are evidenced. Recurrent trains of sub‐vertical truncations on the stoss side of structures reshape and steepen the bedforms. In contrast, sporadic coarse‐grained lenses and lensoidal layers flatten bedforms by filling troughs. The coarsest (clasts up to 10 cm), least sorted and massive structures still exhibit lineation patterns that follow the general backset bedding trend. The stratal architecture exhibits strong lateral variations within tens of centimetres, with very local truncations both in flow‐perpendicular and flow‐parallel directions. This study infers that the sedimentary patterns of bedforms result from four formation mechanisms: (i) differential draping; (ii) slope‐influenced saltation; (iii) truncative bursts; and (iv) granular‐based events. Whereas most of the literature makes a straightforward link between backset bedding and Froude‐supercritical flows, this interpretation is reconsidered here. Indeed, features that would be diagnostic of subcritical dunes, antidunes and 'chute and pools' can be found on the same horizon and in a single bedform, only laterally separated by short distances (tens of centimetres). These data stress the influence of the pulsating and highly turbulent nature of the currents and the possible role of coherent flow structures such as Görtler vortices. Backset bedding is interpreted here as a consequence of a very high sedimentation environment of weak and waning currents that interact with the pre‐existing morphology. Quantification of near‐bed flow velocities is made via comparison with wind tunnel experiments. It is estimated that shear velocities of ca 0·30 m.s−1 (equivalent to pure wind velocity of 6 to 8 m.s−1 at 10 cm above the bed) could emplace the constructive bedsets, whereas the truncative phases would result from bursts with impacting wind velocities of at least 30 to 40 m.s−1. [ABSTRACT FROM AUTHOR]
- Published
- 2019
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3. OSPREY 3.0: Open‐source protein redesign for you, with powerful new features.
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Hallen, Mark A., Martin, Jeffrey W., Ojewole, Adegoke, Jou, Jonathan D., Lowegard, Anna U., Frenkel, Marcel S., Gainza, Pablo, Nisonoff, Hunter M., Mukund, Aditya, Wang, Siyu, Holt, Graham T., Zhou, David, Dowd, Elizabeth, and Donald, Bruce R.
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PROTEIN engineering ,GRAPHICS processing units ,OPEN source software ,PYTHON programming language ,COMPUTER algorithms - Abstract
We present osprey 3.0, a new and greatly improved release of the osprey protein design software. Osprey 3.0 features a convenient new Python interface, which greatly improves its ease of use. It is over two orders of magnitude faster than previous versions of osprey when running the same algorithms on the same hardware. Moreover, osprey 3.0 includes several new algorithms, which introduce substantial speedups as well as improved biophysical modeling. It also includes GPU support, which provides an additional speedup of over an order of magnitude. Like previous versions of osprey, osprey 3.0 offers a unique package of advantages over other design software, including provable design algorithms that account for continuous flexibility during design and model conformational entropy. Finally, we show here empirically that osprey 3.0 accurately predicts the effect of mutations on protein–protein binding. Osprey 3.0 is available at http://www.cs.duke.edu/donaldlab/osprey.php as free and open‐source software. © 2018 Wiley Periodicals, Inc. We present the third major release of the OSPREY protein design software, along with comparisons to experimental data that confirm its ability to optimize protein mutants for desired functions. Osprey 3.0 has significant efficiency, ease‐of‐use, and algorithmic improvements over previous versions, including GPU acceleration and a new Python interface. [ABSTRACT FROM AUTHOR]
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- 2018
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4. Fast search algorithms for computational protein design.
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Traoré, Seydou, Roberts, Kyle E., Allouche, David, Donald, Bruce R., André, Isabelle, Schiex, Thomas, and Barbe, Sophie
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SEARCH algorithms ,PROTEIN engineering ,AMINO acid sequence ,COMBINATORIAL optimization ,COST functions ,ALGORITHMS - Abstract
One of the main challenges in computational protein design (CPD) is the huge size of the protein sequence and conformational space that has to be computationally explored. Recently, we showed that state-of-the-art combinatorial optimization technologies based on Cost Function Network (CFN) processing allow speeding up provable rigid backbone protein design methods by several orders of magnitudes. Building up on this, we improved and injected CFN technology into the well-established CPD package Osprey to allow all Osprey CPD algorithms to benefit from associated speedups. Because Osprey fundamentally relies on the ability of [ABSTRACT FROM AUTHOR]
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- 2016
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5. Fast gap-free enumeration of conformations and sequences for protein design.
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Roberts, Kyle E., Gainza, Pablo, Hallen, Mark A., and Donald, Bruce R.
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ABSTRACT Despite significant successes in structure-based computational protein design in recent years, protein design algorithms must be improved to increase the biological accuracy of new designs. Protein design algorithms search through an exponential number of protein conformations, protein ensembles, and amino acid sequences in an attempt to find globally optimal structures with a desired biological function. To improve the biological accuracy of protein designs, it is necessary to increase both the amount of protein flexibility allowed during the search and the overall size of the design, while guaranteeing that the lowest-energy structures and sequences are found. DEE/A*-based algorithms are the most prevalent provable algorithms in the field of protein design and can provably enumerate a gap-free list of low-energy protein conformations, which is necessary for ensemble-based algorithms that predict protein binding. We present two classes of algorithmic improvements to the A* algorithm that greatly increase the efficiency of A*. First, we analyze the effect of ordering the expansion of mutable residue positions within the A* tree and present a dynamic residue ordering that reduces the number of A* nodes that must be visited during the search. Second, we propose new methods to improve the conformational bounds used to estimate the energies of partial conformations during the A* search. The residue ordering techniques and improved bounds can be combined for additional increases in A* efficiency. Our enhancements enable all A*-based methods to more fully search protein conformation space, which will ultimately improve the accuracy of complex biomedically relevant designs. Proteins 2015; 83:1859-1877. © 2015 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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6. Improved energy bound accuracy enhances the efficiency of continuous protein design.
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Roberts, Kyle E. and Donald, Bruce R.
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ABSTRACT Flexibility and dynamics are important for protein function and a protein's ability to accommodate amino acid substitutions. However, when computational protein design algorithms search over protein structures, the allowed flexibility is often reduced to a relatively small set of discrete side-chain and backbone conformations. While simplifications in scoring functions and protein flexibility are currently necessary to computationally search the vast protein sequence and conformational space, a rigid representation of a protein causes the search to become brittle and miss low-energy structures. Continuous rotamers more closely represent the allowed movement of a side chain within its torsional well and have been successfully incorporated into the protein design framework to design biomedically relevant protein systems. The use of continuous rotamers in protein design enables algorithms to search a larger conformational space than previously possible, but adds additional complexity to the design search. To design large, complex systems with continuous rotamers, new algorithms are needed to increase the efficiency of the search. We present two methods, PartCR and HOT, that greatly increase the speed and efficiency of protein design with continuous rotamers. These methods specifically target the large errors in energetic terms that are used to bound pairwise energies during the design search. By tightening the energy bounds, additional pruning of the conformation space can be achieved, and the number of conformations that must be enumerated to find the global minimum energy conformation is greatly reduced. Proteins 2015; 83:1151-1164. © 2015 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]
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- 2015
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7. Systematic solution to homo-oligomeric structures determined by NMR.
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Martin, Jeffrey W., Zhou, Pei, and Donald, Bruce R.
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ABSTRACT Protein structure determination by NMR has predominantly relied on simulated annealing-based conformational search for a converged fold using primarily distance constraints, including constraints derived from nuclear Overhauser effects, paramagnetic relaxation enhancement, and cysteine crosslinkings. Although there is no guarantee that the converged fold represents the global minimum of the conformational space, it is generally accepted that good convergence is synonymous to the global minimum. Here, we show such a criterion breaks down in the presence of large numbers of ambiguous constraints from NMR experiments on homo-oligomeric protein complexes. A systematic evaluation of the conformational solutions that satisfy the NMR constraints of a trimeric membrane protein, DAGK, reveals 9 distinct folds, including the reported NMR and crystal structures. This result highlights the fundamental limitation of global fold determination for homo-oligomeric proteins using ambiguous distance constraints and provides a systematic solution for exhaustive enumeration of all satisfying solutions. Proteins 2015; 83:651-661. © 2015 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]
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- 2015
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8. Dead-end elimination with perturbations (DEEPer): A provable protein design algorithm with continuous sidechain and backbone flexibility.
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Hallen, Mark A., Keedy, Daniel A., and Donald, Bruce R.
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Computational protein and drug design generally require accurate modeling of protein conformations. This modeling typically starts with an experimentally determined protein structure and considers possible conformational changes due to mutations or new ligands. The DEE/A* algorithm provably finds the global minimum-energy conformation (GMEC) of a protein assuming that the backbone does not move and the sidechains take on conformations from a set of discrete, experimentally observed conformations called rotamers. DEE/A* can efficiently find the overall GMEC for exponentially many mutant sequences. Previous improvements to DEE/A* include modeling ensembles of sidechain conformations and either continuous sidechain or backbone flexibility. We present a new algorithm, DEEPer ( Dead- End Elimination with Perturbations), that combines these advantages and can also handle much more extensive backbone flexibility and backbone ensembles. DEEPer provably finds the GMEC or, if desired by the user, all conformations and sequences within a specified energy window of the GMEC. It includes the new abilities to handle arbitrarily large backbone perturbations and to generate ensembles of backbone conformations. It also incorporates the shear, an experimentally observed local backbone motion never before used in design. Additionally, we derive a new method to accelerate DEE/A*-based calculations, indirect pruning, that is particularly useful for DEEPer. In 67 benchmark tests on 64 proteins, DEEPer consistently identified lower-energy conformations than previous methods did, indicating more accurate modeling. Additional tests demonstrated its ability to incorporate larger, experimentally observed backbone conformational changes and to model realistic conformational ensembles. These capabilities provide significant advantages for modeling protein mutations and protein-ligand interactions. Proteins 2013. © 2012 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]
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- 2013
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9. Protein loop closure using orientational restraints from NMR data.
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Tripathy, Chittaranjan, Zeng, Jianyang, Zhou, Pei, and Donald, Bruce Randall
- Abstract
Protein loops often play important roles in biological functions. Modeling loops accurately is crucial to determining the functional specificity of a protein. Despite the recent progress in loop prediction approaches, which led to a number of algorithms over the past decade, few rigorous algorithmic approaches exist to model protein loops using global orientational restraints, such as those obtained from residual dipolar coupling (RDC) data in solution nuclear magnetic resonance (NMR) spectroscopy. In this article, we present a novel, sparse data, RDC-based algorithm, which exploits the mathematical interplay between RDC-derived sphero-conics and protein kinematics, and formulates the loop structure determination problem as a system of low-degree polynomial equations that can be solved exactly, in closed-form. The polynomial roots, which encode the candidate conformations, are searched systematically, using provable pruning strategies that triage the vast majority of conformations, to enumerate or prune all possible loop conformations consistent with the data; therefore, completeness is ensured. Results on experimental RDC datasets for four proteins, including human ubiquitin, FF2, DinI, and GB3, demonstrate that our algorithm can compute loops with higher accuracy, a three- to six-fold improvement in backbone RMSD, versus those obtained by traditional structure determination protocols on the same data. Excellent results were also obtained on synthetic RDC datasets for protein loops of length 4, 8, and 12 used in previous studies. These results suggest that our algorithm can be successfully applied to determine protein loop conformations, and hence, will be useful in high-resolution protein backbone structure determination, including loops, from sparse NMR data. Proteins 2012. © 2011 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]
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- 2012
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10. A graphical method for analyzing distance restraints using residual dipolar couplings for structure determination of symmetric protein homo-oligomers.
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Martin, Jeffrey W., Yan, Anthony K., Bailey-Kellogg, Chris, Zhou, Pei, and Donald, Bruce R.
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High-resolution structure determination of homo-oligomeric protein complexes remains a daunting task for NMR spectroscopists. Although isotope-filtered experiments allow separation of intermolecular NOEs from intramolecular NOEs and determination of the structure of each subunit within the oligomeric state, degenerate chemical shifts of equivalent nuclei from different subunits make it difficult to assign intermolecular NOEs to nuclei from specific pairs of subunits with certainty, hindering structural analysis of the oligomeric state. Here, we introduce a graphical method, , for the analysis of intermolecular distance restraints and structure determination of symmetric homo-oligomers using residual dipolar couplings. Based on knowledge that the symmetry axis of an oligomeric complex must be parallel to an eigenvector of the alignment tensor of residual dipolar couplings, we can represent distance restraints as annuli in a plane encoding the parameters of the symmetry axis. Oligomeric protein structures with the best restraint satisfaction correspond to regions of this plane with the greatest number of overlapping annuli. This graphical analysis yields a technique to characterize the complete set of oligomeric structures satisfying the distance restraints and to quantitatively evaluate the contribution of each distance restraint. We demonstrate our method for the trimeric E. coli diacylglycerol kinase, addressing the challenges in obtaining subunit assignments for distance restraints. We also demonstrate our method on a dimeric mutant of the immunoglobulin-binding domain B1 of streptococcal protein G to show the resilience of our method to ambiguous atom assignments. In both studies, computed oligomer structures with high accuracy despite using ambiguously assigned distance restraints. [ABSTRACT FROM AUTHOR]
- Published
- 2011
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11. The minimized dead-end elimination criterion and its application to protein redesign in a hybrid scoring and search algorithm for computing partition functions over molecular ensembles.
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Georgiev, Ivelin, Lilien, Ryan H., and Donald, Bruce R.
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PROTEIN engineering ,PROTEINS ,LIGAND binding (Biochemistry) ,CONFORMATIONAL analysis ,ALGORITHMS - Abstract
One of the main challenges for protein redesign is the efficient evaluation of a combinatorial number of candidate structures. The modeling of protein flexibility, typically by using a rotamer library of commonly-observed low-energy side-chain conformations, further increases the complexity of the redesign problem. A dominant algorithm for protein redesign is dead-end elimination (DEE), which prunes the majority of candidate conformations by eliminating rigid rotamers that provably are not part of the global minimum energy conformation (GMEC). The identified GMEC consists of rigid rotamers (i.e., rotamers that have not been energy-minimized) and is thus referred to as the rigid-GMEC. As a postprocessing step, the conformations that survive DEE may be energy-minimized. When energy minimization is performed after pruning with DEE, the combined protein design process becomes heuristic, and is no longer provably accurate: a conformation that is pruned using rigid-rotamer energies may subsequently minimize to a lower energy than the rigid-GMEC. That is, the rigid-GMEC and the conformation with the lowest energy among all energy-minimized conformations (the minimized-GMEC) are likely to be different. While the traditional DEE algorithm succeeds in not pruning rotamers that are part of the rigid-GMEC, it makes no guarantees regarding the identification of the minimized-GMEC. In this paper we derive a novel, provable, and efficient DEE-like algorithm, called minimized-DEE (MinDEE), that guarantees that rotamers belonging to the minimized-GMEC will not be pruned, while still pruning a combinatorial number of conformations. We show that MinDEE is useful not only in identifying the minimized-GMEC, but also as a filter in an ensemble-based scoring and search algorithm for protein redesign that exploits energy-minimized conformations. We compare our results both to our previous computational predictions of protein designs and to biological activity assays of predicted protein mutants. Our provable and efficient minimized-DEE algorithm is applicable in protein redesign, protein-ligand binding prediction, and computer-aided drug design. © 2008 Wiley Periodicals, Inc. J Comput Chem, 2008 [ABSTRACT FROM AUTHOR]
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- 2008
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12. A complete algorithm to resolve ambiguity for intersubunit NOE assignment in structure determination of symmetric homo-oligomers.
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Potluri, Shobha, Yan, Anthony K., Donald, Bruce R., and Bailey-Kellogg, Chris
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Assignment of nuclear Overhauser effect (NOE) data is a key bottleneck in structure determination by NMR. NOE assignment resolves the ambiguity as to which pair of protons generated the observed NOE peaks, and thus should be restrained in structure determination. In the case of intersubunit NOEs in symmetric homo-oligomers, the ambiguity includes both the identities of the protons within a subunit, and the identities of the subunits to which they belong. This paper develops an algorithm for simultanous intersubunit NOE assignment and C
n symmetric homo-oligomeric structure determinations, given the subunit structure. By using a configuration space framework, our algorithm guarantees completeness, in that it identifies structures representing, to within a user-defined similarity level, every structure consistent with the available data (ambiguous or not). However, while our approach is complete in considering all conformations and assignments, it avoids explicit enumeration of the exponential number of combinations of possible assignments. Our algorithm can draw two types of conclusions not possible under previous methods: (1) that different assignments for an NOE would lead to different structural classes, or (2) that it is not necessary to uniquely assign an NOE, since it would have little impact on structural precision. We demonstrate on two test proteins that our method reduces the average number of possible assignments per NOE by a factor of 2.6 for MinE and 4.2 for CCMP. It results in high structural precision, reducing the average variance in atomic positions by factors of 1.5 and 3.6, respectively. [ABSTRACT FROM AUTHOR]- Published
- 2007
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13. Structure determination of symmetric homo-oligomers by a complete search of symmetry configuration space, using NMR restraints and van der Waals packing.
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Potluri, Shobha, Yan, Anthony K., Chou, James J., Donald, Bruce R., and Bailey-Kellogg, Chris
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Structural studies of symmetric homo-oligomers provide mechanistic insights into their roles in essential biological processes, including cell signaling and cellular regulation. This paper presents a novel algorithm for homo-oligomeric structure determination, given the subunit structure, that is both complete, in that it evaluates all possible conformations, and data-driven, in that it evaluates conformations separately for consistency with experimental data and for quality of packing. Completeness ensures that the algorithm does not miss the native conformation, and being data-driven enables it to assess the structural precision possible from data alone. Our algorithm performs a branch-and-bound search in the symmetry configuration space, the space of symmetry axis parameters (positions and orientations) defining all possible C
n homo-oligomeric complexes for a given subunit structure. It eliminates those symmetry axes inconsistent with intersubunit nuclear Overhauser effect (NOE) distance restraints and then identifies conformations representing any consistent, well-packed structure to within a user-defined similarity level. For the human phospholamban pentamer in dodecylphosphocholine micelles, using the structure of one subunit determined from a subset of the experimental NMR data, our algorithm identifies a diverse set of complex structures consistent with the nine intersubunit NOE restraints. The distribution of determined structures provides an objective characterization of structural uncertainty: backbone RMSD to the previously determined structure ranges from 1.07 to 8.85 Å, and variance in backbone atomic coordinates is an average of 12.32 Å2 . Incorporating vdW packing reduces structural diversity to a maximum backbone RMSD of 6.24 Å and an average backbone variance of 6.80 Å2 . By comparing data consistency and packing quality under different assumptions of oligomeric number, our algorithm identifies the pentamer as the most likely oligomeric state of phospholamban, demonstrating that it is possible to determine the oligomeric number directly from NMR data. Additional tests on a number of homo-oligomers, from dimer to heptamer, similarly demonstrate the power of our method to provide unbiased determination and evaluation of homo-oligomeric complex structures. Proteins 2006. © 2006 Wiley-Liss, Inc. [ABSTRACT FROM AUTHOR]- Published
- 2006
- Full Text
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14. A subgroup algorithm to identify cross-rotation peaks consistent with non-crystallographic symmetry.
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Lilien, Ryan H., Bailey-Kellogg, Chris, Anderson, Amy C., and Donald, Bruce R.
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X-ray crystallography ,CRYPTOSPORIDIUM ,LEISHMANIA ,OPTICAL diffraction ,ASYMMETRIC synthesis ,STANDARD deviations ,IONIZING radiation ,ALGORITHMS - Abstract
Molecular replacement (MR) often plays a prominent role in determining initial phase angles for structure determination by X-ray crystallography. In this paper, an efficient quaternion-based algorithm is presented for analyzing peaks from a cross-rotation function in order to identify model orientations consistent with proper non-crystallographic symmetry (NCS) and to generate proper NCS-consistent orientations missing from the list of cross-rotation peaks. The algorithm, CRANS, analyzes the rotation differences between each pair of cross-rotation peaks to identify finite subgroups. Sets of rotation differences satisfying the subgroup axioms correspond to orientations compatible with the correct proper NCS. The CRANS algorithm was first tested using cross-rotation peaks computed from structure-factor data for three test systems and was then used to assist in the de novo structure determination of dihydrofolate reductase-thymidylate synthase (DHFR-TS) from Cryptosporidium hominis. In every case, the CRANS algorithm runs in seconds to identify orientations consistent with the observed proper NCS and to generate missing orientations not present in the cross-rotation peak list. The CRANS algorithm has application in every molecular-replacement phasing effort with proper NCS. [ABSTRACT FROM AUTHOR]
- Published
- 2004
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15. Thin Film RuO2 Lithiation: Fast Lithium‐Ion Diffusion along the Interface.
- Author
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Kim, Sungkyu, Evmenenko, Guennadi, Xu, Yaobin, Buchholz, Donald Bruce, Bedzyk, Michael, He, Kai, Wu, Jinsong, and Dravid, Vinayak P.
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LITHIUM-ion batteries ,CONVERSION disorder ,DEFENSE mechanisms (Psychology) ,HYSTERIA ,SOMATOFORM disorders - Abstract
Although lithium‐ion batteries that run on the conversion reaction have high capacity, their cyclability remains problematic due to large volume changes and material pulverization. Dimensional confinement, such as 2D thin film or nanodots in a conductive matrix, is proposed as a way of improving the cyclic stability, but the lithiation mechanism of such dimensionally controlled materials remains largely unknown. Here, by in situ transmission electron microscopy, lithiation of thin RuO2 films with different thicknesses and directions of lithium‐ion diffusion are observed at atomic resolution to monitor the reactions. From the side‐wall diffusion in ≈4 nm RuO2 film, the ion‐diffusion and reaction are fast, called "interface‐dominant" mode. In contrast, in ≈12 nm film, the ion diffusion–reaction only occurs at the interface where there is a high density of defects due to misfits between the film and substrate, called the "interface‐to‐film" mode. Compared to the side‐wall diffusion, the reaction along the normal direction of the thin film are found to be sluggish ("layer‐to‐layer" mode). Once lithiation speed is higher, the volume expansion is larger and the intercalation stage becomes shorter. Such observation of preferential lithiation direction in 2D‐like RuO2 thin film provides useful insights to develop dimensionally confined electrodes for lithium‐ion batteries. The electrochemical lithiation of epitaxial‐grown RuO2 films with different thickness and directions of lithium‐ion diffusion is investigated using the in situ high resolution transmission electron microscopy (HRTEM) technique. The observation of preferential lithiation direction and the different volume expansion in 2D‐like RuO2 thin film provides useful insights to develop dimensionally confined electrodes for lithium‐ion batteries. [ABSTRACT FROM AUTHOR]
- Published
- 2018
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16. The Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Reveals a Novel Architecture for the Bifunctional Enzyme.
- Author
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O'Neil, Robert H., Lilien, Ryan H., Donald, Bruce R., Stroud, Robert M., and Anderson, Amy C.
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CRYPTOSPORIDIUM ,PEPTIDE hormones ,CRYPTOSPORIDIUM parvum ,GENETICS - Abstract
Examines the crystal structure of dihydrofolate reductase-thymidylate synthase (DHFR-TS) from Cryptosporidium hominis. Association between DHFR and TS domains; Importance of the linker polypeptide between the structural interaction of DHFR and TS; Residue substitutions between DHFR-TS of C. homonis and C. parvum.
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- 2003
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17. Dingwell, Head Receive 2013 N. L. Bowen Award: Response.
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Dingwell, Donald Bruce
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- 2014
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