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Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Protein Stabiliity.'
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Veenstra, D. L., and P. A. Kollman. "Modeling protein stability: a theoretical analysis of the stability of T4 lysozyme mutants." Protein Engineering Design and Selection 10, no. 7 (July 1, 1997): 789–807. http://dx.doi.org/10.1093/protein/10.7.789.
Kim, Yoo-Gon, Woo-Jong Lee, Chan-Hee Won, Yong-Hee Kim, Ji-Sun Yun, Min-Seon Hong, and Chul-Soo Shin. "A study on short-term stability of recombinant protein A." Analytical Science and Technology 24, no. 3 (June 25, 2011): 193–99. http://dx.doi.org/10.5806/ast.2011.24.3.193.
Tomczyńska-Mleko, M. "Structure and stability of ion induced whey protein aerated gels." Czech Journal of Food Sciences 31, No. 3 (May 22, 2013): 211–16. http://dx.doi.org/10.17221/247/2012-cjfs.
The microstructure and stability of aerated whey protein gels were determined. Foamed whey protein gels were obtained using a novel method applying a simultaneous gelation and aeration process. Whey protein gels were produced at different protein concentrations and pH by calcium ion induction at ambient temperature. Two concentrations of calcium ions were used: 20 and 30mM to produce foamed gels with different microstructure. Foamed gels obtained at 30mM Ca<sup>2+</sup> were composed of thick strands and irregular, large air bubbles. For these gels, larger synaeresis and bubble size reduction were observed. Fine-stranded, small bubble size aerated gels obtained at 20mM Ca<sup>2+</sup> were very stable during storage. Decreased protein concentration and increased pH of the gels resulted in an increased bubble size.
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Arnone, M. I., L. Birolo, S. Pascarella, M. V. Cubellis, F. Bossa, G. Sannia, and G. Marino. "Stability of aspartate aminotransferase from Sulfolobus solfataricus." Protein Engineering Design and Selection 10, no. 3 (March 1, 1997): 237–48. http://dx.doi.org/10.1093/protein/10.3.237.
Greene, Lesley H., Jay A. Grobler, Vladimir A. Malinovskii, Jie Tian, K. Ravi Acharya, and Keith Brew. "Stability, activity and flexibility in α-lactalbumin." Protein Engineering, Design and Selection 12, no. 7 (July 1999): 581–87. http://dx.doi.org/10.1093/protein/12.7.581.
Brems, David N., Patricia L. Brown, Christopher Bryant, Ronald E. Chance, L. Kenney Green, Harlan B. Long, Alita A. Miller, Rohn Millican, James E. Shields, and Bruce H. Frank. "Improved insulin stability through amino acid substitution." "Protein Engineering, Design and Selection" 5, no. 6 (1992): 519–25. http://dx.doi.org/10.1093/protein/5.6.519.
Rajalakshmi, N., and P. V. Sundaram. "Stability of native and covalently modified papain." "Protein Engineering, Design and Selection" 8, no. 10 (1995): 1039–47. http://dx.doi.org/10.1093/protein/8.10.1039.
Chin, I. S., A. M. A. Murad, N. M. Mahadi, S. Nathan, and F. D. A. Bakar. "Thermal stability engineering of Glomerella cingulata cutinase." Protein Engineering Design and Selection 26, no. 5 (March 6, 2013): 369–75. http://dx.doi.org/10.1093/protein/gzt007.
Takano, K., and K. Yutani. "A new scale for side-chain contribution to protein stability based on the empirical stability analysis of mutant proteins." Protein Engineering Design and Selection 14, no. 8 (August 1, 2001): 525–28. http://dx.doi.org/10.1093/protein/14.8.525.
Dissertations / Theses on the topic "Protein Stabiliity":
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Malinka, František. "Strojové učení v úloze predikce vlivu aminokyselinových mutací na stabilitu proteinu." Master's thesis, Vysoké učení technické v Brně. Fakulta informačních technologií, 2014. http://www.nusl.cz/ntk/nusl-236035.
This thesis describes a new approach to the detection of protein stability change upon amino acid mutations. The main goal is to create a new meta-tool, which combines the outputs of eight well-established prediction tools and due to suitable method of consensus making, it is able to improve the overall prediction accuracy. The optimal strategy of combination of outputs of these tools is found by using a various number of machine learning methods. From all tested machine learning methods, KStar showed the highest prediction accuracy on the training dataset compiled from experimentally validated mutations originating from ProTherm database. Due to this reason, it is chosen as an optimal prediction technique. The general prediction abilities is validated on the testing dataset composed of multi-point amino acid mutations extracted also from ProTherm database. Since the multi-point mutations were not used for training any of integrated tools, we suppose that such comparison is objective. As a result, the developed meta-tool based on KStar technique improves the correlation coefficient about 0.130 on the training dataset and 0.239 on the testing dataset, respectively (the comparison is being made against the most succesful integrated tool). Based on the obtained results, it is possible to claim that machine learning methods are suitable technique for the problems from area of protein predictions.
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Agah, Sayeh. "Parvalbumin stability and calcium affinity : the impact of the n-terminal domain /." Free to MU Campus, others may purchase, 2004. http://wwwlib.umi.com/cr/mo/fullcit?3164486.
Rubin, Jonathan. "Ion-specific and water-mediated effects on protein physical stability." Diss., Georgia Institute of Technology, 2013. http://hdl.handle.net/1853/47587.
Protein aggregation and physical stability are perpetual concerns in medicine and industry. Misfolded protein can form ordered protein aggregates, amyloids, which are associated with a host of neurodegenerative diseases in mammals and control heritable traits in fungi and yeast. Industrially, amorphous aggregates reduce the efficacy of protein-based therapeutics and activity of enzymes during production and storage. This work studies ion-specific and solvent-based effects on protein physical stability. We show that ion-specificity significantly affects amyloid formation kinetics, aggregate morphology, thermostability, frangibility, and, most intriguingly, prion infectivity in vivo. Forming amyloid in chaotropic or kosmotropic solutions generates predominately weak or strong prion variants, respectively. Ion-specific effects also influenced amorphous aggregation of model proteins and antibodies. To quantify protein - protein stability/affinity, we developed a rapid and reliable diffusion-based technique. Our technique was able to resolve relative differences in colloidal stability between various saline and saccharide solutions. In all, this dissertation expands our understanding of ion-specific and water-mediated interactions with prion proteins and protein dispersions.
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Pothier, Laura J. "Effects of amino acid substitutions on the conformation and stability of A[beta]₁₆₋₂₂ aggregates /." Connect to online version, 2007. http://ada.mtholyoke.edu/setr/websrc/pdfs/www/2007/213.pdf.
Verma, Kusum S. "The osmotic second virial coefficient as a predictor of protein stability." Master's thesis, Mississippi State : Mississippi State University, 2006. http://sun.library.msstate.edu/ETD-db/ETD-browse/browse.
Katayama, Derrick S. "Towards a mechanistic understanding of pharmaceutical protein stabilization in solution and the solid state /." Connect to full text via ProQuest. Limited to UCD Anschutz Medical Campus, 2006.
Thesis (Ph.D. in Pharmaceutical Sciences) -- University of Colorado at Denver and Health Sciences Center, 2006. Typescript. Includes bibliographical references (leaves 159-173). Free to UCDHSC affiliates. Online version available via ProQuest Digital Dissertations;
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Bianco, Carolina. "Role of nonionic surfactants in promoting the folding and stability of integral membrane proteins." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 317 p, 2008. http://proquest.umi.com/pqdweb?did=1612981801&sid=12&Fmt=2&clientId=8331&RQT=309&VName=PQD.
Thesis (Ph.D.)--University of Delaware, 2008. Principal faculty advisors: Eric W. Kaler, College of Engineering; and Abraham M. Lenhoff, Dept. of Chemical Engineering. Includes bibliographical references.
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Agius, R. "Understanding stability of protein-protein complexes." Thesis, University College London (University of London), 2015. http://discovery.ucl.ac.uk/1462393/.
For all living organisms, macromolecular interactions facilitate most of their natural functions. Alterations to macromolecular structures through mutations, can affect the stability of their interactions, which may lead to unfavourable phenotypes and disease. Presented here, are a number of computational methods aimed at uncovering the principles behind complex stability - as described by binding affinity and dissociation rate constants. Several factors are known to govern the stability of protein-protein interactions, however, no one factor dominates, and it is the synergistic effect of a number of contributions, which amount to the affinity, and stability of a complex. The characterization of complex stability can thus be presented as a two-fold problem; modelling the individual factors and modelling the synergistic effect of the combination of such individual factors. Using machine learning as a central framework, empirical functions are designed for estimating affinity, dissociation rates and the effects of mutations on these properties. The performance of all models is in turn benchmarked on experimental data available from the literature and carefully curated datasets. Firstly, a wild-type binding free energy prediction model is designed, composed of a diverse set of stability descriptors, which account for flexibility and conformational changes undergone by the complex in question. Similarly, models for estimating the effects of mutations on binding affinity are also designed and benchmarked in a community-wide blind trial. Emphasis here is on the detection of a small subset of mutations that are able to enhance the stability of two de novo protein drugs targeting the flu virus hemagglutinin. Probing further the determinants of stability, a set of descriptors that link hotspot residues with the off-rate of a complex are designed, and applied to models predicting changes in off-rate upon mutation. Finally, the relationship between the distribution of hotspots at protein interfaces, and the rate of dissociation of such interfaces, is investigated.
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Yasuda, Satoshi. "Studies Based on Statistical Mechanics for Structural Stability of Proteins and Protein Complexes." Kyoto University, 2013. http://hdl.handle.net/2433/174741.
Morozov, Alexandre V. "Free energy functions in protein structural stability and folding kinetics /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/9690.
Chemical Congress of North America (4th 1991 New York, N.Y.). Biocatalyst design for stability and specificity. Edited by Himmel Michael E, Georgiou George, American Chemical Society. Division of Biochemical Technology., and American Chemical Society Meeting. Washington, DC: American Chemical Society, 1993.
Franks, Felix. "Conformational Stability of Proteins." In Protein Biotechnology, 395–436. Totowa, NJ: Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2_11.
Dill, K. A., and D. O. V. Alonso. "Conformational Entropy and Protein Stability." In Protein Structure and Protein Engineering, 51–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74173-9_6.
Jaenicke, Rainer. "Protein Stability and Protein Folding." In Ciba Foundation Symposium 161 - Protein Conformation, 206–21. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514146.ch13.
Ó’Fágáin, Ciarán. "Engineering Protein Stability." In Methods in Molecular Biology, 103–36. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-913-0_7.
Pfeil, Wolfgang. "Introduction." In Protein Stability and Folding, 1–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-12838-1_1.
Pfeil, W. "Introduction." In Protein Stability and Folding, 3–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58760-3_1.
Copeland, Robert A. "Protein Folding and Stability." In Methods for Protein Analysis, 199–216. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4757-1505-7_10.
McCammon, J. Andrew, Chung F. Wong, and Terry P. Lybrand. "Protein Stability and Function." In Prediction of Protein Structure and the Principles of Protein Conformation, 149–59. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-1571-1_4.
Conference papers on the topic "Protein Stabiliity":
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Truskett, Thomas M. "How Concentration and Crowding Impact Protein Stability: Insights From a Coarse-Grained Model." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192239.
Much of the current understanding of the protein folding problem derives from studies of proteins in dilute solutions. However, in many systems of scientific and engineering interest, proteins must fold in concentrated, heterogeneous environments. Cells are crowded with many molecular species, and chaperones often sequester proteins and promote rapid folding. Proteins are also present in high concentrations in the manufacture, storage, and delivery of biotherapeutics. How does crowding generally affect the stability of the native state? Are all crowding agents created equal? If not, can generic structural or chemical features forecast their effects on protein stability?
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Nottingham, Elizabeth M., Michelle G. Zeles-Hahn, and Corinne S. Lengsfeld. "Understanding EHDA and Protein Stability." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176708.
Therapeutic proteins can be difficult to work with due to the fact that each protein has properties and functions that are unique. These exclusive properties are in part due to the proteins three-dimensional shape (secondary and tertiary structure). This shape is determined by bends in the amino acid sequence generated by electrostatic interactions, hydrogen bonds, and hydrophobic-hydrophilic interactions between neighboring amino acids. These bonding interactions are weak and can be severed by chemical or physical forces. Thus, therapeutic proteins can be denatured during manufacture and by methods used to deliver them to the body.
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Li, Dai-xi, and Xiaoming He. "Desiccation Dependent Structure and Stability of an Anhydrobiotic Nematode Late Embryogenesis Abundant (LEA) Protein." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206862.
A number of organisms have been found to be capable of surviving severe water deficit as a result of extreme drought and cold in nature by entering a state of suspended animation (i.e., anhydrobiosis or life without water) [1]. Although the precise molecular repertoire of desiccation tolerance in anhydrobiotic organisms is still not fully understood, results from recent studies indicate the crucial role of stress proteins such as the late embryogenesis abundant (LEA) proteins [2]. LEA proteins have been proposed to play a variety of roles in protecting biologicals from damaging by dehydration stress such as molecular chaperone and shield, ion chelator, antioxidant, and space filler. The multifunctional capacity of LEA proteins has been attributed in part to their structural plasticity: they are unfolded and when fully hydrated and become folded during water deficit [1]. However, the structural stability of LEA protein in response to desiccation is still not fully understood. In this study, the structure alteration of a group 3 LEA protein from an anhydrobiotic nematode (AavLEA1) [2] were investigated using the molecular dynamics (MD) simulation approach to understand the structural stability at different water contents.
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Cuppoletti, John. "Composite Synthetic Membranes Containing Native and Engineered Transport Proteins." In ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2008. http://dx.doi.org/10.1115/smasis2008-449.
Our membrane transport protein laboratory has worked with material scientists, computational chemists and electrical and mechanical engineers to design bioactuators and sensing devices. The group has demonstrated that it is possible to produce materials composed native and engineered biological transport proteins in a variety of synthetic porous and solid materials. Biological transport proteins found in nature include pumps, which use energy to produce gradients of solutes, ion channels, which dissipate ion gradients, and a variety of carriers which can either transport substances down gradients or couple the uphill movement of substances to the dissipation of gradients. More than one type of protein can be reconstituted into the membranes to allow coupling of processes such as forming concentration gradients with ion pumps and dissipating them with an ion channel. Similarly, ion pumps can provide ion gradients to allow the co-transport of another substance. These systems are relevant to bioactuation. An example of a bioactuator that has recently been developed in the laboratory was based on a sucrose-proton exchanger coupled to a proton pump driven by ATP. When coupled together, the net reaction across the synthetic membrane was ATP driven sucrose transport across a flexible membrane across a closed space. As sucrose was transported, net flow of water occurred, causing pressure and deformation of the membrane. Transporters are regulated in nature. These proteins are sensitive to voltage, pH, sensitivity to a large variety of ligands and they can be modified to gain or lose these responses. Examples of sensors include ligand gated ion channels reconstituted on solid and permeable supports. Such sensors have value as high throughput screening devices for drug screening. Other sensors that have been developed in the laboratory include sensors for membrane active bacterial products such as the anthrax pore protein. These materials can be self assembled or manufactured by simple techniques, allowing the components to be stored in a stable form for years before (self) assembly on demand. The components can be modified at the atomic level, and are composed of nanostructures. Ranges of sizes of structures using these components range from the microscopic to macroscopic scale. The transport proteins can be obtained from natural sources or can be produced by recombinant methods from the genomes of all kingdoms including archea, bacteria and eukaryotes. For example, the laboratory is currently studying an ion channel from a thermophile from deep sea vents which has a growth optimum of 90 degrees centigrade, and has membrane transport proteins with very high temperature stability. The transport proteins can also be genetically modified to produce new properties such as activation by different ligands or transport of new substances such as therapeutic agents. The structures of many of these proteins are known, allowing computational chemists to help understand and predict the transport processes and to guide the engineering of new properties for the transport proteins and the composite membranes. Supported by DARPA and USARMY MURI Award and AFOSR.
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Frau, Eleonora, and Silvia Schintke. "Towards Standards for Light Scattering Studies of Proteins Stability and Nanoparticle-Protein Interactions." In 2020 22nd International Conference on Transparent Optical Networks (ICTON). IEEE, 2020. http://dx.doi.org/10.1109/icton51198.2020.9203371.
Qiu, Weiguo, Joseph Cappello, and Xiaoyi Wu. "Fabrication of Genetically Engineered Silk-Elastin-Like Protein Polymer Fibers." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-190980.
Micro- and submicro-diameter protein fibers are fundamental building blocks of extra- and intra-cellular matrices, providing structural support, stability and protection to cells, tissues and organism [1]. Fabricating performance fibers of both naturally derived and genetically engineered proteins has been extensively pursued for a variety of biomedical applications, including tissue engineering and drug delivery [2]. Silk-elastin-like proteins (SELPs), consisting of tandemly repeated polypeptide sequences derived from silk and elastin, have been biosynthesized using recombinant DNA technique [3]. Their potential as a biomaterials in the form of hydrogels continues to be explored [4, 5]. This study will focus on the fabrication of robust, micro-diameter SELP fibers as biomaterials for tissue engineering applications.
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Koç, Mehmet, Emine Varhan, Zehra Kasımoğlu, and Hilal Şahin Nadeem. "The effect of different wall materials on the production of suppressed-pungent capsaicin microparticles." In 21st International Drying Symposium. Valencia: Universitat Politècnica València, 2018. http://dx.doi.org/10.4995/ids2018.2018.7721.
The aim of this study was to investigate the effects of wall materials types on the production of double-layered and suppressed-pungent capsaicin microparticles via spray chilling method. For this purpose, palm oil and different proteins (gelatin, sodium caseinate and whey protein) were used as wall materials, while soy lecithin was selected as stabilizer. Sample encapsulated only with palm oil (single-layered) was used as control. Centrifuge stability and kinetic stability were analyzed on the prepared emulsions. Total and surface capsaicin, microencapsulation efficiency, melting point temperature and fusion enthalpy analysis were carried out on the capsaicin microparticles obtained by spray chilling.Keywords: Capsaicin; Spray chilling method; Pungency; Double-layered microparticles
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Tchebotarev, L., and L. Valentovich. "Engineering of vectors essential to derive chimeric proteins based on superfolder green fluorescent protein and harpins." In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.245.
Conjugation of harpins with green fluorescent protein is aimed at achieving enhanced solubility and stability of chimeric protein, facilitating qualitative and quantitative evaluation of its expression in the routine experiments.
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Van Nostrand, W. E., and P. P. Cunningham. "PROTEASE NEXIN II IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643490.
Normal human fibroblasts secrete a protein into the culture medium named protease nexin II (PN II), which forms sodium do-decyl sulfate (SDS)-stable complexes with epidermal growth factor binding protein (EGF BP). These complexes then bind back to the same cells and are rapidly internalized and degraded. We recently purified PN II to apparent homogeneity and showed that it is a single chain polypeptide with an estimated molecular weight of 106 KDa. Other interesting properties of this protein include its ability to bind heparin and its stability to treatment with SDS or pH 1.5. In addition to EGF BP, PN II will also complex the gamma subunit of 7S nerve growth factor (NGF-gamma) and trypsin. Here we show that human platelets contain a protein which possesses the same properties as does PN II from cultured human fibroblasts. This platelet PN II (PL-PN II) is also a 106 KDa single chain polypeptide which can complex EGF BP, NGF-gamma and trypsin. PL-PN II also possesses the unusual stability to treatment with SDS or pH 1.5. In addition, both PN II and PL-PN II exhibit the same affinity for binding to heparin-Sepharose. Furthermore, rabbit polyclonal antiserum raised against PN II recognized PL-PN II on Western blot analysis demonstrating that both proteins are immunologically related. Treatment of fresh unactivated platelets with epinephrine or thrombin resulted in a release of PL-PN II into the supernatant suggesting that PL-PN II is stored in the platelet alpha granules.
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Xu, Mengyang, D. K. George, R. Jimenez, and A. G. Markelz. "Nondestructive determination of protein structural stability." In 2017 42nd International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz). IEEE, 2017. http://dx.doi.org/10.1109/irmmw-thz.2017.8067017.
Eichler, Jerry. Protein Glycosylation in Archaea: A Post-Translational Modification to Enhance Extremophilic Protein Stability. Fort Belvoir, VA: Defense Technical Information Center, January 2010. http://dx.doi.org/10.21236/ada515568.
Ellis, J., A. E. Faraggi, and D. V. Nanopoulos. M-theory model-building and proton stability. Office of Scientific and Technical Information (OSTI), September 1997. http://dx.doi.org/10.2172/541933.
McHugh, Colleen A., Ralph F. Tammariello, Charles B. Millard, and John H. Carra. Improved Stability of a Protein Vaccine Through Elimination of a Partially Unfolded State. Fort Belvoir, VA: Defense Technical Information Center, January 2004. http://dx.doi.org/10.21236/ada428734.
Thirumalai, Devarajan. Principles Governing the Stability and Folding Kinetics of Proteins From Extremophiles. Fort Belvoir, VA: Defense Technical Information Center, January 2012. http://dx.doi.org/10.21236/ada567225.
Davis, Ryan W., James A. Brozik, Susan Marie Brozik, Jason M. Cox, Gabriel P. Lopez, Todd A. Barrick, and Adrean Flores. Nanoporous microbead supported bilayers: stability, physical characterization, and incorporation of functional transmembrane proteins. Office of Scientific and Technical Information (OSTI), March 2007. http://dx.doi.org/10.2172/902211.
Boris Merinov, William A. Goddard III, Sossina Haile, Adri van Duin, Peter Babilo, and Sang Soo Han. Enhanced Power Stability for Proton Conducting Solid Oxides Fuel Cells. Office of Scientific and Technical Information (OSTI), December 2005. http://dx.doi.org/10.2172/877384.
Belaguli, Narasimhaswamy S. Forkhead Box Protein 1 (Foxa1) and the Sumoylation Pathway that Regulates Foxa1 Stability are Potential Targets for Breast Cancer Treatment. Fort Belvoir, VA: Defense Technical Information Center, September 2007. http://dx.doi.org/10.21236/ada489768.
K. Y. Ng. Space charge and beam stability issues of the Fermilab proton driver in Phase I. Office of Scientific and Technical Information (OSTI), August 2001. http://dx.doi.org/10.2172/784993.
Meth, M. Stability of screen and grid power supplies for the RF power amplifier for proton cavity. Office of Scientific and Technical Information (OSTI), December 1987. http://dx.doi.org/10.2172/1150481.
Boris Merinov, Sossina Haile, and William A. Goddard III. Enhanced Power Stability for Proton Conducting Solid Oxides Fuel Cells. Calculated energy barriers for proton diffusion in Y-doped BaZrO3. Potential electrode materials for application in proton ceramic fuel cells. Office of Scientific and Technical Information (OSTI), April 2005. http://dx.doi.org/10.2172/876771.
