Relevant bibliographies by topics / Biochemical reactions

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Biochemical reactions'

Author: Grafiati
Published: 4 June 2021
Last updated: 7 February 2022

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Journal articles on the topic "Biochemical reactions"

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Chisti, Yusuf. "What drives biochemical reactions?" Biotechnology Advances 22, no. 4 (February 2004): 309–10. http://dx.doi.org/10.1016/j.biotechadv.2003.10.001.

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Mathews, Christopher K. "Thermodynamics of biochemical reactions." Biochemistry and Molecular Biology Education 32, no. 1 (January 2004): 444. http://dx.doi.org/10.1002/bmb.2004.494032019999.

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Bühler, M., and C. Wandrey. "Oleochemicals by Biochemical Reactions?" Fett Wissenschaft Technologie/Fat Science Technology 94, no. 3 (1992): 82–94. http://dx.doi.org/10.1002/lipi.19920940303.

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Alberty, Robert A. "Constraints in biochemical reactions." Biophysical Chemistry 49, no. 3 (April 1994): 251–61. http://dx.doi.org/10.1016/0301-4622(93)e0075-g.

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Villadsen, John. "Simulation of biochemical reactions." Computers & Chemical Engineering 13, no. 4-5 (April 1989): 385–95. http://dx.doi.org/10.1016/0098-1354(89)85018-5.

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HESS, BENNO. "Periodic patterns in biochemical reactions." Quarterly Reviews of Biophysics 30, no. 2 (May 1997): 121–76. http://dx.doi.org/10.1017/s003358359700334x.

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Schramm, Vern L. "Chemical Mechanisms in Biochemical Reactions." Journal of the American Chemical Society 133, no. 34 (August 31, 2011): 13207–12. http://dx.doi.org/10.1021/ja2062314.

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Edwards, D. A. "Biochemical Reactions on Helical Structures." SIAM Journal on Applied Mathematics 60, no. 4 (January 2000): 1425–46. http://dx.doi.org/10.1137/s0036139998343769.

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NAKAMURA, K. "Biochemical reactions in supercritical fluids." Trends in Biotechnology 8 (1990): 288–92. http://dx.doi.org/10.1016/0167-7799(90)90200-h.

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Yang, Bin, Chuan Zhu Liao, Ming Yan Jiang, and Dong Feng Yuan. "Delayed Stochastic Biochemical Reactions Reconstruction Based on Additive Reaction Model." Advanced Materials Research 894 (February 2014): 280–83. http://dx.doi.org/10.4028/www.scientific.net/amr.894.280.

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Stochastic dynamics and delayed time of biochemical reactions play an important role in the biological networks such as gene regulatory and metabolic networks. This paper presents a new model, called additive reaction model (ARM), to capture the stochastic dynamical and delayed behavior. The new evolutionary strategy is used to search the optimal biochemical model, in which genetic algorithm (GA) and particle swarm optimization (PSO) are employed to evolve the architecture and parameters of biochemical reactions, respectively. The results reveal that the delayed biochemical reaction modeling problems could be solved effectively and efficiently using our proposed new model and new evolutionary strategy.
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Dissertations / Theses on the topic "Biochemical reactions"

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Fradet, Etienne. "Monitoring biochemical reactions in stationary droplets." Palaiseau, Ecole polytechnique, 2013. http://pastel.archives-ouvertes.fr/docs/00/92/97/15/PDF/fradet_thesis_2013.pdf.

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La microfluidique de gouttes - i. E. L'emploi de gouttelettes comme microréacteurs - offre de nombreux avantages pour l'étude des systèmes biologiques. Dans ce travail de thèse, nous présentons une nouvelle approche pour la production et la manipulation de gouttelettes au sein de microcanaux afin de suivre l'avancement de réactions biochimiques au cours du temps. Contrairement aux approches existantes, notre dispositif utilise des gradients de confinement afin de produire et guider une unique goutte vers son lieu de stockage. Ce faisant, deux gouttes de contenus différents peuvent être appariées et fusionnées afin de déclencher une réaction chimique. Les réactifs n'étant pas activement mélangés, un front de réaction se propage alors le long de la goutte fille duquel on peut extraire la cinétique de la réaction. Nous commençons par l'étude de réactions simples ayant lieu en une étape. Un modèle 1D de réaction-diffusion permet de représenter la dynamique du front de réaction ce qui est vérifié en confrontant les solutions de ce modèle, obtenues numériquement ou analytiquement, à des mesures effectuées en gouttes. Puis, nous nous intéressons au cas des réactions enzymatiques. Nous démontrons d'abord la parallélisation de notre technique d'appariement de gouttes afin de reproduire en microcanal différents tests enzymatiques usuellement effectués en plaque multipuits. Finalement, nous étudions le cas des réactions enzymatiques rapides à l'aide de notre modèle de réaction-diffusion. Là encore, la comparaison d'expériences tenues en gouttes et de prédiction issues de notre modèle nous permet d'extraire une mesure des paramètres cinétiques de la réaction mise en jeu
Droplet microfluidics - i. E. The use of droplets as microreactors - offers significant advantages for the study of biological systems. In this work, we present a new platform for the production and manipulation of microfluidic droplets in view of measuring the evolution of biochemical reactions. Contrary to existing approaches, our device uses gradients of confinement to produce a single drop on demand and guide it to a pre-determined location. In this way, two nanoliter drops containing different reagents can be placed in contact and merged together in order to trigger a chemical reaction. Then, an analysis of the observed reaction front yields the reaction rate. We start with the case of one step reactions. We derive a one dimensional reaction-diffusion model for the reaction front and compare numerical and analytical solutions of our model to experiments held in our microsystem. Then, we turn our attention to the case of enzymatic reactions. First, we show how the device operation can be parallelized in order to react an initial sample with a range of compounds or concentrations and we perform standard well-mixed enzyme assays with our parallelized chip, thereby mimicking titer plate assays in droplets. Second, we build onto our reaction-diffusion model to predict the rate of fast enzymatic reactions held in our device. Again, numerical and analytical solutions of our model are compared to experiments done in droplets which yields measurements of the kinetic parameters of the reaction at play
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Marrone, April. "THE BIOCHEMICAL REACTIONS OF DRY STATE DNA." Doctoral diss., University of Central Florida, 2009. http://digital.library.ucf.edu/cdm/ref/collection/ETD/id/3622.

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The biochemistry of dry state DNA is of interest to the fields of forensics, ancient DNA, and DNA storage. The exact chemical nature of the degradation of the DNA molecule in the dry state has not been studied prior. If determined what chemical changes the DNA molecule undergoes, to what degree and in what time frame then protocols can be implemented to bypass the impact of this damage or to repair it when necessary. It is suspected that similar reactions occur to the dry state DNA molecule as does to the hydrated molecule. It cannot be assumed, however that these types of chemical processes occur to the same extent and at the same rates. In general the generic process of hydrolysis encompasses two important reactions, that of deamination and of base loss from the 2’-deoxyribose backbone. Base loss is believed to ultimately lead to chain scission. It is also suspect that reactive oxygen species (ROS) have an important role in the chemistry associated with DNA. Species such as hydroxyl radicals (OH·) and singlet oxygen (¹O₂) can lead to strand scissions and chemically modified bases. Throughout this project various techniques were used to determine damage to DNA and its molecular constituents under conditions leading to hydrolytic and oxidative damage. Novel techniques used in this study include ion-pairing chromatography and denaturing HPLC (DHPLC) to measure glycosidic bond cleavage and strand breaks. The extent to which the macromolecule haemoglobin (Hb) can lead to oxidative damage of DNA in dried blood stains by acting as a Fenton chemistry catalyst was evaluated. Additionally the enzymatic activity of the extracellular nuclease from Alteromonas espejiana, BAL 31 was studied as it pertains to the degradation of single-stranded short homopolymeric oligonucleotides. This study serves as the basis for future, more in depth experimentation into the more specific nature of dry state DNA biochemistry. It was found that to a large extent the same degradation reactions (base hydrolysis, base modifications, and strand breaks) do occur in the dry state as in the hydrated state when heat and UV radiation are used as energy sources. Reaction rates indicate that base hydrolysis and deamination occur much more slowly, yet have the same energies of activation in both states. Single strand breaks of dry state duplex DNA occur with a half life of 24 ± 2 days and appears to occur in a mechanistic manner which could be of interest when attempting to repair such damage. In addition, base loss alone does not correlate with the extent of single strand breaks detected. Thermodynamic data can lead to the conclusion that DNA degradation in both dry and hydrated states is not a spontaneous process. It is also concluded that though the Hb molecule undergoes oxidative changes over time, these changes do not impact its ability to become a more aggressive Fenton reagent. However, the presence of Hb in the vicinity of DNA does create the opportunity for OH· induced damage to the deoxyribose sugar, and most likely the DNA bases themselves. This study also reveals that the general purpose BAL 31 nuclease commonly used in molecular genetics exhibits a hithertofore non-characterized degree of substrate specificity with respect to single-stranded DNA oligomers. Specifically, BAL 31 nuclease activity was found to be affected by the presence of guanine in ssDNA oligomers.
Ph.D.
Department of Chemistry
Sciences
Chemistry PhD
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Mistry, Dharmit. "Mechanistic studies of some chemical and biochemical reactions." Thesis, University of Huddersfield, 2014. http://eprints.hud.ac.uk/id/eprint/23444/.

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Three aspects of chemical and biochemical reactions were investigated. 1. The relative reactivities of pyrophosphate (phosphorus(V)) and pyro-di-H-phosphonate (phosphorus(III)) and its derivatives have been analysed at various pHs. The hydrolysis rate of pyro-di-H-phosphonate (PP(III)) was found to be higher than pyrophosphate at all pHs. Using ITC and NMR, pyrophosphate showed metal-ion complexing abilities whereas pyro-di-H-phosphonate showed weak or no complexing to metal-ions, although the rate of hydrolysis at pH 7 slightly increased compared to the spontaneous hydrolysis of PP(III). The enzymatic hydrolysis of pyrophosphate, which is thought to occur via MgPP(V)2-, occurs efficiently and is close to being diffusion controlled. Pyro-di-H-phosphonate on the other hand does not act as a substrate or as an inhibitor of pyrophosphatase. 2. Dichloromethane (DCM) is an alkylating agent for pyridine, producing methylene bis-pyridinium dication (MDP) upon refluxing the solution. The kinetics and mechanism of hydrolysis of methylene bis-pyridinium dication have been studied. Below pH 7 MDP is extremely stable and hydrolysis is first-order in hydroxide-ion. Above pH 9 an unusual intermediate is formed on hydrolysis which has a chromophore at 366 nm in water and its formation is second-order in hydroxide-ion. The carbon acidity of the central methylene group was also investigated kinetically using H/D exchange and the pKa was surprisingly high at 21.2 at 25oC (I = 1.0 M). 3. Isothermal titration calorimetry (ITC) is a technique mainly used by biochemists to obtain a range of physical and thermodynamic properties of a reaction. Analysing the data can become difficult when investigating complex reactions involving more than one step, for instance metal-ions binding to an enzyme. In this work models have been developed to simulate sequential reactions. These were used to simulate experimental ITC data for metal-ions: Zn2+, Co2+ and Cd2+ complexing to the active sites of BcII, a metallo β-lactamase responsible for antibiotic resistance, providing additional information on the mechanism by which this enzyme acts to deactivate β-lactam antibiotics. The simulations suggest that BcII has two very similar binding affinities to metal-ions which are filled sequentially.
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Dubey, Nidhi Chandrama. "Smart hydrogels based platforms for investigation of biochemical reactions." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-184082.

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Polyketides are natural products with complex chemical structures and immense pharmaceutical potential that are synthesized via secondary metabolic pathways. The in-vitro synthesis of these molecules requires high supply of building blocks such as acetyl Co-enzyme A, and cofactors (adenosine triphosphate (ATP). These precursor and cofactor are synthesized from respective soluble enzymes. Owing to the expensive nature of the enzymes, it is important to immobilize enzymes to improve the process economics by enabling multiple uses of catalyst and improving overall productivity and robustness. The polymer-based particles of nano and submicron size have become attractive material for their role in the life sciences. With the advances in synthetic protocols of the microgels and commercial availability of many of the monomers, it is feasible to tune the properties of the particles as per the process requirement. The core shell microgel with functional shell allows high loading of ligands onto the microgel particles due to increased availability of functional group on the outer surface. The aim of the thesis thus was to study biochemical reactions on the smart microgels support using single (acetyl CoA synthetase (Acs)) and dual (pyruvate kinase (Pk) and L-lactic dehydrogenase (Ldh)) enzyme/s systems. The study indicated that the enzyme immobilization significantly depends on the enzyme, conjugation strategy and the support. The covalent immobilization provides rigidity to the enzyme structure as in case of Acs immobilized on PNIPAm-AEMA microgels but at the same time leads to loss in enzyme activity. Whereas, in the case of covalent immobilization of Ldh on microgel showed improved in enzyme activity. On the other hand adsorption of the enzyme via ionic interaction provide better kinetic profile of enzymes hence the membrane reactor was prepared using PNIPAm-PEI conjugates for acetyl CoA synthesis. The better outcome of work with PNIPAm-PEI resulted in its further evaluation for dual enzyme system. This work is unique in the view that the immobilization strategies were well adapted to immobilize single and dual enzymes to achieve stable bioconjugates for their respective applications in precursor biosynthesis (Acetyl Co enzyme A) and co-factor dependent processes (ACoA and ATP). The positive end results of microgels as the support (particles in solution and as the thin film (membrane)) opens further prospective to explore these systems for other precursor biomolecule production.
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Davis, Aaron Vincent Tarn. "Chemical and Biochemical Redox Reactions of the Anticancer Drug Streptonigrin." Thesis, Queen Mary, University of London, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.504553.

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Streptonigrin has shown activity against several tumours (e.g. breast and lung). The drug induces cytotoxicity by impairing DNA synthesis via inhibition of Topoisomerase II and direct damage to DNA through attack by ROS (reactive oxygen species), the latter of which has been linked to the aminoquinone domain [Bolzc'm and Bianchi 2001]. Streptonigrin exists in one of three possible oxidation states, the oxidised quinone, the le- reduced semiquinone radical and a 2e- reduced hydroquinone. The semiquinone radical has been linked to the production of ROS species through redox cycling in the presence of oxygen. The superoxide and hydroxyl radicals cause damage to various cellular constituents e.g. proteins and nucleic acids (HO· is the primary source of the drug's toxicity). In addition to this streptonigrin has a high affinity for different metal ions e.g. iron and copper. The drug-metal complexes are known to increase streptonigrin's binding affinity to DNA [Bolzfm and Bianchi 2001]. Little is known about the effects of the metal on the chemical and biological activity of the drug. Most of the research on the redox chemistry of streptonigrin (SN) has consisted of NMR studies of SN metal complexes in organic solvents at concentrations which are not feasible at physiological conditions. This research focused on determining the precise mechanism involved in streptonigrin semiquinone formation; the precise role of different metal ions in semiquinone formation and the affect of different pH via two buffers with different pHs (5.5 and 9.5). The experimental data showed that semiquinone formation occurred via complete reduction followed by oxidation rather than I e- reduction . Subsequent EPR experiments also confirmed that metal ions had a direct affect on semlqumone formatIon, wuh streptol1lgrm metal bmdmg ratios greater than I: I mhlbumg semiquinone formation. Experiments carried out to measure reactive oxygen species formation by the drug showed limited evidence of superoxide formation by the different drug metal complexes; however there was clear evidence of hydroxyl radical formation which appeared to change in concentration with metal ion concentration in a similar fashion to the semiquinone. The experimental work should assist future drug analogue development.
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Greenfield, Daniel Leo Computer Science &amp Engineering Faculty of Engineering UNSW. "New and hybrid methods for simulating biochemical systems." Awarded by:University of New South Wales. Computer Science and Engineering, 2006. http://handle.unsw.edu.au/1959.4/23990.

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It is a dream of Systems-Biology to efficiently simulate an entire cell on a computer. The potential medical and biological applications of such a tool are immense, and so are the challenges to accomplish it. At the level of a cell, the number of reacting molecules is so low that stochastic effects can be crucial in deciding the system-level behaviour of the cell. Despite the recent development of many new and hybrid stochastic approaches, exact stochastic simulation algorithms are still needed, and are widely employed in most current biochemical simulation packages. Unfortunately, the performance of these algorithms scales badly with the number of reactions. It is shown that this is especially the case for hubs and scale-free networks. This is worrying because hubs are an important component of biochemical systems, and it is widely suspected that biochemical networks are scale-free. It is shown that the scalability issue in these algorithms is due to the high interdependency between reactions. A general method for arbitrarily reducing this interdependency is introduced, and it is shown how it can be used for many classes of simulation processes. This is applied to one of the fastest algorithms currently, the Next Reaction Method. The resulting algorithm, the Reactant-Margin Method, is tested on a wide range of hub sizes and shown to be asymptotically faster than the current best algorithms. Hybrid versions of the Reactant-Margin Method and the Next Reaction Method are also compared on a real biological model - the Lambda-Phage virus, and the new algorithm is again shown to perform better. The problems inherent in the hybridization are also shown to be more exactly and efficiently handled in the Reactant-Margin framework than in the Next-Reaction Method framework. Finally, a software tool called GeNIV is introduced. This GUI-based biochemical modelling and simulation tool is an embodiment of a mechanistic-representation philosophy. It is implements the Reactant Margin and Next Reaction hybrid algorithms, and has a simple representation system for gene-state occupancy and their subsequent biochemical reactions. It is also novel in that it translates the graphical model into Javacode which is compiled and executed for simulation.
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Liu, Yang, and 刘洋. "Free energy simulations of important biochemical processes." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2013. http://hdl.handle.net/10722/196036.

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Free energy simulations have been widely employed to compute the thermodynamic properties of many important biochemical processes. In the first part of this dissertation, two important biochemical processes, protonation/deprotonation of acid in solution and solvation of small organic molecules, are investigated using free energy simulations. Accurate computation of the pKa value of a compound in solution is important and challenging. To efficiently simulate the free energy change associated with the protonation/deprotonation processes in solution, a new method of mixing Hamiltonian, implemented as an approach using a fractional protonin the hybrid quantum mechanics/molecular mechanics (QM/MM) scheme, is developed. This method is a combination of a large class of λ-coupled free-energy simulation methods and the linear combination of atomic potential approach. Theoretical and technical details of this method, along with the calculation results of the pKa value of methanol and methanethiol molecules in aqueous solution, are discussed. The simulation results show satisfactory agreement with experimental data. Though the QM/MM method is one of the most useful methods in the modeling of biochemical processes, little attention has been paid to the accuracy of QM/MM methods as an integrated unit. Therefore, the solvation free energies of a set of small organic molecules are simulated as an assessment of ab initio QM/MM methods. It shows that the solvation free energy from QM/MM simulations can vary over a broad range depending on the level of QM theory / basis sets employed. Diffuse functions tend to over-stabilize the solute molecules in aqueous solution. The deviations pose a pressing challenge to the future development of new generation of MM force fields and QM/MM methods if consistency with QM methods becomes a natural requirement. In the second part of the dissertation, the dynamic and energetic properties of two molten globule (MG) protein molecules, α-lactalbumin(α-LA) and monomeric chorismate mutase (mCM) are investigated using molecular dynamics simulations. The exploring of the molecular mechanism of protein folding is a never-settled battle while the properties of MG states and their roles in protein folding become an important question. The MGs show increased side chain flexibility while maintain comparable side-chain coupling compared to the native state, which partially explains the preserving of native-like overall conformation. The enhanced sampling method, temperature-accelerated molecular dynamics (TAMD), is used for the study of the hydrophobic interactions inside both biomolecules. The results suggest that these hydrophobic cores could overcome energy barriers and repack into new conformation states with even lower energies. The repacking of the hydrophobic cores in MGs might be served as a criterion for recognizing the MGs in large class of biomolecules.
published_or_final_version
Chemistry
Doctoral
Doctor of Philosophy
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Möller, Mark. "A hybrid algorithm for the simulation of biochemical reactions and diffusion." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=982994052.

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Gomez, David [Verfasser], and Stefan [Akademischer Betreuer] Klumpp. "Mechanisms of biochemical reactions within crowded environments / David Gomez ; Betreuer: Stefan Klumpp." Potsdam : Universität Potsdam, 2016. http://d-nb.info/1218400757/34.

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Rajanayagam, Kavitha. "Chemical and biochemical redox reactions of the anthra quinone anticancer drug Mitoxantrone." Thesis, Queen Mary, University of London, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.417075.

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Books on the topic "Biochemical reactions"

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Thermodynamics of biochemical reactions. Cambridge, MA: Massachusetts Institute of Technology, 2003.

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Alberty, Robert A. Thermodynamics of Biochemical Reactions. New York: John Wiley & Sons, Ltd., 2005.

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Alberty, Robert A. Thermodynamics of Biochemical Reactions. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2003. http://dx.doi.org/10.1002/0471332607.

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Zaikov, G. E. Chemical and biochemical reactions: Kinetics and mechanism. New York: Nova Science, 2011.

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Schügerl, Karl. Bioreaction engineering: Reactions involving microorganisms and cells. Chichester: Wiley, 1987.

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Sonochemistry: Theory, reactions, syntheses, and applications. Hauppauge, N.Y: Nova Science Publishers, 2009.

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D, Litmanovich Arkady, and Noah Olga V, eds. Macromolecular reactions: Peculiarities, theory, and experimental approaches. Chichester: J. Wiley, 1995.

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Orru, Romano V. A. Synthesis of Heterocycles via Multicomponent Reactions II. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2010.

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Jackson, A. T. Process engineering in biotechnology. Milton Keynes: Open University Press, 1990.

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Process engineering in biotechnology. Englewood Cliffs, N.J: Prentice Hall, 1991.

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Book chapters on the topic "Biochemical reactions"

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Keener, James, and James Sneyd. "Biochemical Reactions." In Interdisciplinary Applied Mathematics, 1–47. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-75847-3_1.

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Zacheo, Giuseppe. "Biochemical Reactions and Interactions." In Cyst Nematodes, 163–77. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2251-1_9.

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Ehrenfeucht, Andrzej, and Grzegorz Rozenberg. "Biochemical Reactions as Computations." In Lecture Notes in Computer Science, 672–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-73001-9_70.

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Malar, Carlin Geor, Muthulingam Seenuvasan, and Kannaiyan Sathish Kumar. "Diffusion Limitations in Biocatalytic Reactions." In Biochemical and Environmental Bioprocessing, 139–50. First edition. | Boca Raton, FL : CRC Press/Taylor & Francis Group, 2020.: CRC Press, 2019. http://dx.doi.org/10.1201/9780429198045-8.

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Chakraborty, Suman. "Electrokinetic Transport with Biochemical Reactions." In Encyclopedia of Microfluidics and Nanofluidics, 845–58. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-5491-5_432.

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Nielsen, Jens, John Villadsen, and Gunnar Lidén. "Biochemical Reactions — A First Look." In Bioreaction Engineering Principles, 47–93. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0767-3_3.

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Ehrenfeucht, A., and G. Rozenberg. "Modeling Interactions between Biochemical Reactions." In Applications and Theory of Petri Nets, 7. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-68746-7_2.

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Formighieri, Cinzia. "Downstream Biochemical Reactions: Carbon Assimilation." In SpringerBriefs in Environmental Science, 59–63. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16730-5_12.

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Chappell, Michael, and Stephen Payne. "Cell Structure and Biochemical Reactions." In Biosystems & Biorobotics, 1–18. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-26197-3_1.

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Nakamura, K. "Biochemical reactions in supercritical fluids." In Supercritical Fluid Processing of Food and Biomaterials, 54–61. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2169-3_4.

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Conference papers on the topic "Biochemical reactions"

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Haugen, Doug G. "Instrument for monitoring biochemical reactions." In Spectroscopy '90, 4-6 June, Los Cruces, edited by Bernard J. McNamara and Jeremy M. Lerner. SPIE, 1990. http://dx.doi.org/10.1117/12.22113.

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Singh, Abhyudai, and Joao Pedro Hespanha. "Lognormal Moment Closures for Biochemical Reactions." In Proceedings of the 45th IEEE Conference on Decision and Control. IEEE, 2006. http://dx.doi.org/10.1109/cdc.2006.376994.

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Huang, De-An, Jie-Hong R. Jiang, Ruei-Yang Huang, and Chi-Yun Cheng. "Compiling program control flows into biochemical reactions." In the International Conference. New York, New York, USA: ACM Press, 2012. http://dx.doi.org/10.1145/2429384.2429462.

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Hanna, Hanna Abo, Loai Danial, Shahar Kvatinsky, and Ramez Daniel. "Modeling biochemical reactions and gene networks with memristors." In 2017 IEEE Biomedical Circuits and Systems Conference (BioCAS). IEEE, 2017. http://dx.doi.org/10.1109/biocas.2017.8325229.

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Hanna, Hanna Abo, Loai Danial, Shahar Kvatinsky, and Ramez Daniel. "Memristors as Artificial Biochemical Reactions in Cytomorphic Systems." In 2018 IEEE International Conference on the Science of Electrical Engineering in Israel (ICSEE). IEEE, 2018. http://dx.doi.org/10.1109/icsee.2018.8645982.

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Nelatury, Sudarshan R., and Mary C. Vagula. "Simulation studies in biochemical signaling and enzyme reactions." In SPIE Sensing Technology + Applications, edited by Šárka O. Southern, Mark A. Mentzer, Isaac Rodriguez-Chavez, and Virginia E. Wotring. SPIE, 2014. http://dx.doi.org/10.1117/12.2053197.

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Wang, Pei, Jinhu Lu, Li Wan, and Yao Chen. "A stochastic simulation algorithm for biochemical reactions with delays." In 2013 7th International Conference on Systems Biology (ISB). IEEE, 2013. http://dx.doi.org/10.1109/isb.2013.6623803.

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Lei Zhang, Tao Dong, Xinyan Zhao, Zhaochu Yang, and N. M. M. Pires. "An infrared radiation based thermal biosensor for enzymatic biochemical reactions." In 2012 34th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2012. http://dx.doi.org/10.1109/embc.2012.6345983.

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Mane, Vibha, Monica F. Bugallo, and Petar M. Djuric. "A stochastic approach to studying biochemical reactions without Monte Carlo simulations." In 2009 IEEE/SP 15th Workshop on Statistical Signal Processing (SSP). IEEE, 2009. http://dx.doi.org/10.1109/ssp.2009.5278518.

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Zhang, Changjiang, Kimberly Forsten-Williams, Michael Fannon, Wensheng Shen, and Jun Zhang. "Parallel simulation of multiple proteins through a bioreactor coupled with biochemical reactions." In the 2nd ACM Conference. New York, New York, USA: ACM Press, 2011. http://dx.doi.org/10.1145/2147805.2147808.

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Reports on the topic "Biochemical reactions"

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Phelps, Michael E. Microfluidic technology platforms for synthesizing, labeling and measuring the kinetics of transport and biochemical reactions for developing molecular imaging probes. Office of Scientific and Technical Information (OSTI), September 2009. http://dx.doi.org/10.2172/1164633.

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Wurl, Oliver. Biofilm-like habitat at the sea-surface: A mesocosm study, Cruise No. POS537, 14.09.2019 – 04.10.2019, Malaga (Spain) – Cartagena (Spain) - BIOFILM. University of Oldenburg, November 2020. http://dx.doi.org/10.3289/cr_pos537.

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Abstract:
OceanRep OceanRep Startseite Kontakt Schnellsuche Einfache Suche Erweiterte Suche Blättern Autor Forschungsbereich Publikationsart Jahr Studiengang Neuzugänge Artikel – begutachtet Alle Über uns GEOMAR Bibliothek Open Access Policies Grundsätze Hilfe FAQs Statistik Impressum Biofilm-like habitat at the sea-surface: A mesocosm study, Cruise No. POS537, 14.09.2019 – 04.10.2019, Malaga (Spain) – Cartagena (Spain) - BIOFILM . Logged in as Heidi Düpow Einträge verwaltenManage recordsManage shelvesProfilGespeicherte SuchenBegutachtungAdminLogout - Tools Wurl, Oliver, Mustaffa, Nur Ili Hamizah, Robinson, Tiera-Brandy, Hoppe, Jennifer, Jaeger, Leonie, Striebel, Maren, Heinrichs, Anna-Lena, Hennings, Laura Margarethe, Goncalves, Rodrigo, Ruiz Gazulla, Carlota und Ferrera, Isabel (2020) Biofilm-like habitat at the sea-surface: A mesocosm study, Cruise No. POS537, 14.09.2019 – 04.10.2019, Malaga (Spain) – Cartagena (Spain) - BIOFILM . Open Access . POSEIDON Berichte . University of Oldenburg, Oldenburg, 35 pp. [img] Text Cruise_Reports_POS537_final.pdf - publizierte Version Available under License Creative Commons: Attribution 4.0. Download (2417Kb) | Vorschau Abstract Biofilm-like properties can form on sea surfaces, but an understanding of the underlying processes leading to the development of these biofilms is not available. We used approaches to study the development of biofilm-like properties at the sea surface, i.e. the number, abundance and diversity of bacterial communities and phytoplankton, the accumulation of gel-like particles and dissolved tracers. During the expedition POS537 we used newly developed and free drifting mesocosms and performed incubation experiments. With these approaches we aim to investigate the role of light and UV radiation as well as the microbes themselves, which lead to the formation of biofilms. With unique microbial interactions and photochemical reactions, sea surface biofilms could be biochemical reactors with significant implications for ocean and climate research, e.g. with respect to the marine carbon cycle, diversity of organisms and oceanatmosphere interactions.
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