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Academic literature on the topic 'Macromolecular'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 March 2023

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Journal articles on the topic "Macromolecular"

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Li, Yue, Jinlian Duan, Heng Xia, Bin Shu, and Weigang Duan. "Macromolecular substances as a dangerous factor in traditional Chinese medicine injections were determined by size-exclusive chromatography." Toxicology Research 9, no. 3 (May 21, 2020): 323–30. http://dx.doi.org/10.1093/toxres/tfaa024.

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Abstract Macromolecular substances in traditional Chinese medicine injections (TCMIs) are expected to be a main dangerous factor causing anaphylactic or anaphylactoid reaction. The main aim of the study was to verify the macromolecular substances’ anaphylactic or anaphylactoid reaction in guinea pigs and establish a size-exclusive chromatographic method to detect them. The macromolecular substances from six TCMIs (Danshen injection, Dengzhanxixin injection, Honghua injection, Qingkailing injection, Shuanghuanglian injection and Shuxuening injection) were prepared by removing substances with molecular weight less than 10 kDa with an ultra-filter. The anaphylactic and anaphylactoid reactions caused by original TCMIs, injections rich in or free of macromolecules were assayed in guinea pigs. The relationship between the amount of the macromolecular substances and peak area of chromatogram was established by size-exclusive chromatography. Injections free of macromolecules were not likely to cause anaphylactic and anaphylactoid reactions, but injections rich in macromolecular substances were more likely to do so. If the macromolecular substances with molecular weight bigger than 10 kDa were removed, the signal of macromolecular substances in TCMIs was quantitatively reduced. All the results suggested that macromolecular substances in TCMIs are a dangerous factor causing safety problems, and the macromolecular substances can be quantitatively detected with size-exclusive chromatography.

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Henneberg, Fabian, and Ashwin Chari. "Chromatography-Free Purification Strategies for Large Biological Macromolecular Complexes Involving Fractionated PEG Precipitation and Density Gradients." Life 11, no. 12 (November 24, 2021): 1289. http://dx.doi.org/10.3390/life11121289.

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A complex interplay between several biological macromolecules maintains cellular homeostasis. Generally, the demanding chemical reactions which sustain life are not performed by individual macromolecules, but rather by several proteins that together form a macromolecular complex. Understanding the functional interactions amongst subunits of these macromolecular machines is fundamental to elucidate mechanisms by which they maintain homeostasis. As the faithful function of macromolecular complexes is essential for cell survival, their mis-function leads to the development of human diseases. Furthermore, detailed mechanistic interrogation of the function of macromolecular machines can be exploited to develop and optimize biotechnological processes. The purification of intact macromolecular complexes is an essential prerequisite for this; however, chromatographic purification schemes can induce the dissociation of subunits or the disintegration of the whole complex. Here, we discuss the development and application of chromatography-free purification strategies based on fractionated PEG precipitation and orthogonal density gradient centrifugation that overcomes existing limitations of established chromatographic purification protocols. The presented case studies illustrate the capabilities of these procedures for the purification of macromolecular complexes.

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Juliano, R. "Challenges to macromolecular drug delivery." Biochemical Society Transactions 35, no. 1 (January 22, 2007): 41–43. http://dx.doi.org/10.1042/bst0350041.

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The use of macromolecules, particularly monoclonal antibodies, as therapeutic agents has come to the forefront in recent years. The biodistribution and delivery issues for protein drugs are shared to a substantial degree with other emerging therapeutic approaches including pharmacologically active nucleic acids and nanoparticles. A generalized approach to these issues involves consideration of the multiple biological barriers that stand between the macromolecular drug or nanoparticle at its site of administration and its ultimate biological target. Considerations of size, stability, non-specific versus specific associations and potency versus toxicity all play a role. The creation of delivery approaches that combine high specificity for the target cell or tissue, high therapeutic payload and modest toxicity remains a challenge, although some very promising examples have emerged recently. A variety of sophisticated targeting strategies, based primarily on combinatorial library methods, when used in combination with new technologies to identify cell-surface receptor ‘signatures’ of specific tissues, will facilitate advances in targeted delivery of macromolecules and nanoparticles. The challenges to contemporary macromolecule drug delivery are complex, thus new research paradigms are emerging that combine the talents of physical and biological scientists to address this key issue for modern pharmacology and therapeutics.

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Hudder, Alice, Lubov Nathanson, and Murray P. Deutscher. "Organization of Mammalian Cytoplasm." Molecular and Cellular Biology 23, no. 24 (December 15, 2003): 9318–26. http://dx.doi.org/10.1128/mcb.23.24.9318-9326.2003.

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ABSTRACT Although the role of macromolecular interactions in cell function has attracted considerable attention, important questions about the organization of cells remain. To help clarify this situation, we used a simple protocol that measures macromolecule release after gentle permeabilization for the examination of the status of endogenous macromolecules. Treatment of Chinese hamster ovary cells with saponin under carefully controlled conditions allowed entry of molecules of at least 800 kDa; however, there were minimal effects on internal cellular architecture and protein synthesis remained at levels comparable to those seen with intact cells. Most importantly, total cellular protein and RNA were released from these cells extremely slowly. The release of actin-binding proteins and a variety of individual cytoplasmic proteins mirrored that of total protein, while marker proteins from subcellular compartments were not released. In contrast, glycolytic enzymes leaked rapidly, indicating that cells contain at least two distinct populations of cytoplasmic proteins. Addition of microfilament-disrupting agents led to rapid and extensive release of cytoplasmic macromolecules and a dramatic reduction in protein synthesis. These observations support the conclusion that mammalian cells behave as highly organized, macromolecular assemblies (dependent on the actin cytoskeleton) in which endogenous macromolecules normally are not free to diffuse over large distances.

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Blakeley, Matthew. "Macromolecular crystallography using neutrons." Biochemist 36, no. 3 (June 1, 2014): 40–42. http://dx.doi.org/10.1042/bio03603040.

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When you think about macromolecular crystallography, the technique that most often comes to mind is X-ray diffraction and it's no wonder. Over 88000 structures of biological macromolecules – from proteins and nucleic acids to viruses and macromolecular assemblies – have been determined using X-rays, and these have contributed significantly to our understanding of a vast array of biological systems and processes.

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Mittal, Shruti, Rimpy Kaur Chowhan, and Laishram Rajendrakumar Singh. "Macromolecular crowding: Macromolecules friend or foe." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 9 (September 2015): 1822–31. http://dx.doi.org/10.1016/j.bbagen.2015.05.002.

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Vohlídal, Jiří, Edward S. Wilks, Andrey Yerin, Alain Fradet, Karl-Heinz Hellwich, Philip Hodge, Jaroslav Kahovec, Werner Mormann, and Robert F. T. Stepto. "Terminology and nomenclature for macromolecular rotaxanes and pseudorotaxanes (IUPAC Recommendations 2012)." Pure and Applied Chemistry 84, no. 10 (September 21, 2012): 2135–65. http://dx.doi.org/10.1351/pac-rec-11-10-15.

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This document provides (i) definitions of terms related to macromolecular rotaxanes and macromolecular pseudorotaxanes and (ii) recommendations for naming these macromolecular assemblies. The nomenclature recommendations presented here have been developed by combining the nomenclature rules for the low-molar-mass (low-M) rotaxanes and those for macromolecules (both established in published IUPAC recommendations) in such a way that the developed nomenclature system provides unambiguous names for macromolecular rotaxanes (and pseudorotaxanes), including differentiation among various isomers of these supramolecular assemblies. Application of the nomenclature recommendations is illustrated using examples covering a wide range of structure types of macromolecular rotaxanes and pseudorotaxanes. An Alphabetical Index of Terms and a List of Abbreviations and Prefixes are included.

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Bazunova, Marina, Valentina Chernova, Roman Lazdin, Angela Shurshina, Anna Bazunova, Mariya Elinson, and Elena Kulish. "Cosolvents Impact on some Properties of the Solutions and the Films of Succinamide Chitosan." Chemistry & Chemical Technology 14, no. 4 (December 15, 2020): 481–86. http://dx.doi.org/10.23939/chcht14.04.481.

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The article deals with the method of the medical purpose materials creation with the controlled physico-chemical and mechanical deformation properties on the basis of water-soluble derivative of amino polysaccharide chitosan – succinamide chitosan. The essence of the method is the macromolecules aggregation processes regulation in the initial solutions by the injection of organic cosolvents – acetone and ethanol. It has been stated that in a mixed solvent succinamide chitosan molecules are not in the form of the isolated macromolecular balls but as the macromolecules interacting (aggregated) systems. It has been proved that the presence of cosolvents decreases the polymer macromolecule links capability to interact with an enzyme and increases physico-mechanical characteristics of the film materials.

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Confer, David R., and Bruce E. Logan. "A conceptual model describing macromolecule degradation by suspended cultures and biofilms." Water Science and Technology 37, no. 4-5 (February 1, 1998): 231–34. http://dx.doi.org/10.2166/wst.1998.0631.

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Macromolecular (> 1,000 daltons) compounds such as proteins and polysaccharides can constitute a significant portion of dissolved organic carbon (DOC) in wastewater, but limited information is available on how these compounds are degraded in suspended and fixed-film biological wastewater treatment systems. Bacteria cannot assimilate intact macromolecules but must first hydrolyze them to monomers or small oligomers. Here, we summarize experiments performed in our laboratory which indicate that the enzymes responsible for hydrolysis are primarily those that remain attached to the cell. In biofilm cultures fed macromolecular substrates, for example, no more than 8% of total hydrolytic activity was found to be located in the cell-free bulk solution. These and other experiments support a generalized mechanism for macromolecule degradation by biofilms that features cell-associated hydrolysis, followed by the release of hydrolytic fragments back into bulk solution. The extent of fragment release is larger for proteins (bovine serum albumin) than for carbohydrates (dextrans).

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Sharp, Kim A. "Analysis of the size dependence of macromolecular crowding shows that smaller is better." Proceedings of the National Academy of Sciences 112, no. 26 (June 15, 2015): 7990–95. http://dx.doi.org/10.1073/pnas.1505396112.

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The aqueous milieu inside cells contains as much as 30–40% dissolved protein and RNA by volume. This large concentration of macromolecules is expected to cause significant deviations from solution ideality. In vivo biochemical reaction rates and equilibria might differ significantly from those measured in the majority of in vitro experiments that are performed at much lower macromolecule concentrations. Consequently crowding, a nonspecific phenomenon believed to arise from the large excluded volume of these macromolecules, has been studied extensively by experimental and theoretical methods. However, the relevant theory has not been applied consistently. When the steric effects of macromolecular crowders and small molecules like water and ions are treated on an equal footing, the effect of the macromolecules is opposite to that commonly believed. Large molecules are less effective at crowding than water and ions. There is also a surprisingly weak dependence on crowder size. Molecules of medium size, ∼5 Å radius, have the same effect as much larger macromolecules like proteins and RNA. These results require a reassessment of observed high-concentration effects and of strategies to mimic in vivo conditions with in vitro experiments.

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Dissertations / Theses on the topic "Macromolecular"

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Mohsin, Huma. "Macromolecular radiopharmaceuticals /." free to MU campus, to others for purchase, 2004. http://wwwlib.umi.com/cr/mo/fullcit?p3164529.

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Kim, Michael F. "Modeling macromolecular assemblies." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2008. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3324618.

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Walter, Thomas S. "Methodology for macromolecular crystallization." Thesis, University of Oxford, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.542989.

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Muthukumar, Murugappan. "Macromolecular translocation through nanopores." Diffusion fundamentals 16 (2011) 6, S. 1, 2011. https://ul.qucosa.de/id/qucosa%3A13734.

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Katsimitsoulia, Zoe. "Macromolecular studies for bionanotechnology." Thesis, University of Oxford, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.559772.

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Conventional computational methods available today for studying macromolecules and their complexes are limited to simulating short time frames and are insufficient to study processes of interest related to their function that usually occur In nature on longer time scales. Alternative methods that extend our capabilities continue to be proposed, and most often involve some kind of reduction In complexity or representation in order to simulate these biological processes on longer time and length scales. The ability to investigate through simulation the structural and functional properties of protein macromolecular complexes IS of particular importance in the field of bionanotechnology, whose goal IS to harness nanoscale devices made from or inspired by biological counterparts. Clearly then, methods are needed that can capture the large changes seen In macromoleculat assemblies to elucidate important principles of their structure and function and apply these to the nanomachines envisaged in bionanotechnology. At the forefront of this field lie the nanomotors, whose biological counterparts, the molecular protein motors, are used in cells to drive a host of essential processes with an amazing degree of efficiency and precision. The work in this thesis describes the development of a hierarchic modeling paradigm applied toward simulating the processi ve movement of the molecular myos m motor protein along an actin filament track. In the hierarchic model, three different levels of protein structure resolution are represented, with the level of detail changing according to the degree of interaction among the molecules, the integrity of which is maintained using a tree of spatially organized bounding volumes. Although applied to an acto-myosin system, the hierarchic framework is general enough so that it may easily be adapted to a number of other biomolecular systems of interest within the bionanotechnology field.

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Muthukumar, Murugappan. "Macromolecular translocation through nanopores." Universitätsbibliothek Leipzig, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-184573.

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Van, De Walle Matthias. "Continuous photoflow for macromolecular design." Thesis, Queensland University of Technology, 2021. https://eprints.qut.edu.au/208293/1/Matthias_Van%20De%20Walle_Thesis.pdf.

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The current thesis critically advances the synthesis of precision macromolecular structures via photochemical approaches. The work examines the use of continuous photoflow setups to facilitate scalable synthesis of various polymeric architectures, and helps to overcome limitations that hinder photochemistry to be incorporated more frequently into industrial processes. This thesis demonstrates the flexibility and versatility of continuous photoflow and its potential to be developed further, to exceed currently existing photochemical procedures based on traditional batch approaches.

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Zhang, Weizhe, and 張蔚哲. "Development of macromolecular phasing methods." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2014. http://hdl.handle.net/10722/206741.

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X-ray crystallography is a powerful method in determining the structure of both small molecules and macromolecules and is now routinely applied in many scientific fields. However, to apply this method, there is an unavoidable problem to tackle: the Phase Problem, which arises because the phases of a scattered x-ray cannot be measured in diffraction experiment and the original structure cannot be retrieved only with the measurable amplitudes. This thesis presents two approaches in the development of macromolecular phasing methods. One approach presented here utilizes molecular envelope of NMR structures for molecular replacement (MR) phasing with the program FSEARCH at low resolution (about 6 Å). X-ray crystallography and NMR are complementary tools in structural biology. However, it is often difficult to use NMR structures as search models in MR to phase crystallographic data. For this purpose, in our study, several targets with both crystallographic and NMR structures available have been tested. The test protocol involves four steps: (1) Model preparation, NMR structures were processed into averaged polyalanine model, and centroid NMR models have also been tested; (2) Six-dimensional low resolution search were carried out by FSEARCH to find the best match between observed and calculated structure factors; (3) Apply the solution (4) Model building and refinement. In our tests, FSEARCH was able to find the correct translation and orientation of the search model in the crystallographic unit cell, while conventional MR procedures were unsuccessful. The other approach presented in this thesis is protein complex structure completion using IPCAS (Iterative Protein Crystal structure Automatic Solution). Protein complexes have been concerned as essential components in almost every cellular process. X-ray crystallography method is quite useful in studying the nature of protein complexes. In this study, we demonstrated a protein complex completion procedure from a partial molecular replacement (MR) solution using IPCAS. IPCAS is a direct-method aided dual-space iterative phasing and model-building procedure. The test cases were carefully selected from a practical perspective and IPCAS could build the whole complex from one or less than one subunit once molecular replacement method could give a partial solution. Before delivering to IPCAS, MR solution model examination and improvement might be necessary. The IPCAS iteration procedure involves (1) real-space model building and refinement; (2) direct-method aided reciprocal-space phase refinement; and (3) phase improvement through density modification. In our tests, IPCAS is able to extend the full length complex from a less than 30% starting model while conventional model building procedure were unsuccessful.
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Frazier, Richard Andrew. "Macromolecular interactions at polysaccharide surfaces." Thesis, University of Nottingham, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.336946.

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Hall, P. J. "The macromolecular chemistry of coals." Thesis, University of Newcastle Upon Tyne, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.377435.

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Books on the topic "Macromolecular"

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Matyjaszewski, Krzysztof, Yves Gnanou, and Ludwik Leibler, eds. Macromolecular Engineering. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2007. http://dx.doi.org/10.1002/9783527631421.

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Chaiken, Irwin, Emilia Chiancone, Angelo Fontana, and Paolo Neri, eds. Macromolecular Biorecognition. Totowa, NJ: Humana Press, 1987. http://dx.doi.org/10.1007/978-1-4612-4600-8.

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Mishra, Munmaya K., Oskar Nuyken, Shiro Kobayashi, Yusuf Yağci, and Bidulata Sar, eds. Macromolecular Engineering. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1905-8.

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Carrondo, Maria Armenia, and Paola Spadon, eds. Macromolecular Crystallography. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-2530-0.

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Hilborn, Jöns G., P. Dubois, C. J. Hawker, J. L. Hedrick, J. G. Hilborn, R. Jérôme, J. Kiefer, J. W. Labadie, D. Mecerreyes, and W. Volksen, eds. Macromolecular Architectures. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/3-540-49196-1.

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W, Carter Charles, and Sweet Robert M, eds. Macromolecular crystallography. San Diego: Academic Press, 1997.

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W, Carter Charles, and Sweet Robert M, eds. Macromolecular crystallography. San Diego: Academic Press, 2003.

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A, Hendrickson Wayne, and Wüthrich Kurt, eds. Macromolecular structures. London: Current Biology, 1992.

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A, Hendrickson Wayne, and Wüthrich Kurt 1938-, eds. Macromolecular structures. London: Current Biology, 1991.

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Harris, J. Robin, and Jon Marles-Wright, eds. Macromolecular Protein Complexes. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-46503-6.

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Book chapters on the topic "Macromolecular"

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Rupp, Bernhard, and Katherine A. Kantardjieff. "Macromolecular Crystallography." In Springer Protocols Handbooks, 821–49. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-375-6_47.

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Matyjaszewski, Krzysztof, Yves Gnanou, and Ludwik Leibler. "Macromolecular Engineering." In Macromolecular Engineering, 1–6. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527631421.ch1.

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Galloway, J. W. "Macromolecular Asymmetry." In Ciba Foundation Symposium 162 - Biological Asymmetry and Handedness, 16–35. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514160.ch3.

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Bory, Benjamin F., and Stefan C. J. Meskers. "Macromolecular Memory." In Emerging Nanoelectronic Devices, 181–93. Chichester, United Kingdom: John Wiley & Sons Ltd, 2014. http://dx.doi.org/10.1002/9781118958254.ch10.

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Coe, F. L., J. H. Parks, and Y. Nakagawa. "Macromolecular Inhibitors." In Urolithiasis, 97–100. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4899-0873-5_28.

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Driscoll, Paul C. "Macromolecular Complexes." In Protein NMR Spectroscopy: Practical Techniques and Applications, 269–317. Chichester, UK: John Wiley & Sons, Ltd, 2011. http://dx.doi.org/10.1002/9781119972006.ch8.

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Gupta, Shipra, and Arunima Verma. "Macromolecular Interactions." In Introduction to Biomolecular Structure and Biophysics, 115–37. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-4968-2_5.

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Isvoran, Adriana, Laura Pitulice, Eudald Vilaseca, Isabel Pastor, Sergio Madurga, and Francesc Mas. "Macromolecular Crowding." In New Frontiers in Nanochemistry, 307–17. Includes bibliographical references and indexes. | Contents: Volume 1. Structural nanochemistry – Volume 2. Topological nanochemistry – Volume 3. Sustainable nanochemistry.: Apple Academic Press, 2020. http://dx.doi.org/10.1201/9780429022951-20.

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Gooch, Jan W. "Dyes, Macromolecular." In Encyclopedic Dictionary of Polymers, 250. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_4152.

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Webster, Owen W. "Group Transfer Polymerization and Its Relationship to Other Living Systems." In Macromolecular Engineering, 1–9. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1905-8_1.

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Conference papers on the topic "Macromolecular"

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Moffat, Keith. "TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHY." In International Conference on Ultrafast Phenomena. Washington, D.C.: OSA, 2000. http://dx.doi.org/10.1364/up.2000.tue1.

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Williams, I. D., B. Merron, R. J. H. Davies, I. G. Hughes, and V. Morozov. "Fragmentation of macromolecular ions." In The fifteenth international conference on the application of accelerators in research and industry. AIP, 1999. http://dx.doi.org/10.1063/1.59193.

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Čevizović, Dalibor, Zoran Ivič, Slobodanka Galovič, Alexei Chizhov, and Alexander Reshetnyak. "Vibron transport in macromolecular chains." In INTERNATIONAL CONFERENCE ON PHYSICAL MESOMECHANICS OF MULTILEVEL SYSTEMS 2014. AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4898887.

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Mansuripur, Masud. "Advances in macromolecular data storage." In SPIE Optical Engineering + Applications, edited by Ryuichi Katayama and Thomas D. Milster. SPIE, 2014. http://dx.doi.org/10.1117/12.2060549.

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Molloy, Kevin, Nasrin Akhter, and Amarda Shehu. "Modeling Macromolecular Structures and Motions." In BCB '18: 9th ACM International Conference on Bioinformatics, Computational Biology and Health Informatics. New York, NY, USA: ACM, 2018. http://dx.doi.org/10.1145/3233547.3233662.

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Andrews, David L., and Robert D. Jenkins. "Energy transfer in macromolecular arrays." In Optical Science and Technology, SPIE's 48th Annual Meeting, edited by Mark G. Kuzyk, Manfred Eich, and Robert A. Norwood. SPIE, 2003. http://dx.doi.org/10.1117/12.502375.

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Winkler, Hanspeter, Jun Liu, Kenneth Taylor, Ping Zhu, and Kenneth Roux. "ELECTRON TOMOGRAPHY OF MACROMOLECULAR ASSEMBLIES." In 2007 4th IEEE International Symposium on Biomedical Imaging: From Nano to Macro. IEEE, 2007. http://dx.doi.org/10.1109/isbi.2007.356833.

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Rohrdanz, Mary A., Wenwei Zheng, Bradley Lambeth, and Cecilia Clementi. "Multiscale characterization of macromolecular dynamics." In XSEDE '13: Extreme Science and Engineering Discovery Environment: Gateway to Discovery. New York, NY, USA: ACM, 2013. http://dx.doi.org/10.1145/2484762.2484836.

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McPherson, Alexander. "Macromolecular crystal growth in microgravity." In Space technology and applications international forum: 1st conference on commercial development of space; 1st conference on next generation launch systems; 2nd spacecraft thermal control symposium; 13th symposium on space nuclear power and propulsion. AIP, 1996. http://dx.doi.org/10.1063/1.49900.

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Walker, D. G., and M. A. Stremler. "Characterization of Chaotic Motion of DNA in Linear Shear Flows." In ASME 2003 International Mechanical Engineering Congress and Exposition. ASMEDC, 2003. http://dx.doi.org/10.1115/imece2003-43699.

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Motion of macromolecules in flows is important to several disciplines such as DNA hybridization studies, self assembly of nanostructures, and transport of suspensions. The present study simulates the motion of macromolecular structures in linear shear flows. A molecular chain is modeled as a coarse-grained series of beads and springs. For a wide range flow conditions, the flow appears chaotic, where quasi-stable limit cycles are observed for several smaller ranges of flow conditions.

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Reports on the topic "Macromolecular"

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Seeman, Nadrian C. Macromolecular Design. Fort Belvoir, VA: Defense Technical Information Center, December 2004. http://dx.doi.org/10.21236/ada428626.

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Forest, M. G. High-Performance Macromolecular Materials. Fort Belvoir, VA: Defense Technical Information Center, March 2006. http://dx.doi.org/10.21236/ada444313.

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Forest, M. G. High-Performance Macromolecular Materials. Fort Belvoir, VA: Defense Technical Information Center, February 2010. http://dx.doi.org/10.21236/ada518688.

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Frechet, Jean M. Macromolecular Antennas and Photovotaics. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada424130.

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Karasz, Frank E. Ultrastructure Processing of Macromolecular Materials. Fort Belvoir, VA: Defense Technical Information Center, November 1990. http://dx.doi.org/10.21236/ada230175.

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Percec, V. From Molecular to Macromolecular Liquid Crystals. Fort Belvoir, VA: Defense Technical Information Center, April 1995. http://dx.doi.org/10.21236/ada293170.

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Furey, W., G. Gilliland, A. McPherson, J. Pflugrath, and G. Vasquez. Macromolecular crystallography, October 14--27, 1997. Office of Scientific and Technical Information (OSTI), December 1997. http://dx.doi.org/10.2172/763988.

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Terwilliger, Thomas C. Statistical density modification in macromolecular crystallography. Office of Scientific and Technical Information (OSTI), February 2011. http://dx.doi.org/10.2172/1052760.

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Jensen, Robert. Conference Macromolecular Transport Across Cellular Membranes"". Fort Belvoir, VA: Defense Technical Information Center, September 2000. http://dx.doi.org/10.21236/ada390726.

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Libera, Matthew R. Quantitative Electron Holography of Macromolecular Structure. Fort Belvoir, VA: Defense Technical Information Center, March 2001. http://dx.doi.org/10.21236/ada392886.

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