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Relevant bibliographies by topics / Enzyme dynamics during catalysis / Dissertations / Theses

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Dissertations / Theses on the topic 'Enzyme dynamics during catalysis'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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1

Nunez, Sara. "Importance of enzyme dynamics in catalysis." Thesis, University of Manchester, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.534144.

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2

Singh, Priyanka. "Enzyme catalysis and dynamics in dihydrofolate reductase." Diss., University of Iowa, 2015. https://ir.uiowa.edu/etd/5635.

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Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate bindings, chemical conversions, and products release. The relationship between protein motions and catalytic activity is of considerable contemporary interest in enzymology. To understand the factors influencing the rates of enzyme catalyzed reactions, the dynamics of the protein-solvent-substrate complex must be considered. The enzyme dihydrofolate reductase from Escherichia coli (EcDHFR) is often used as a model system in various biophysical studies, incl

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3

Dannatt, Hugh. "The role of enzyme dynamics in catalysis by β-phosphoglucomutase". Thesis, University of Sheffield, 2012. http://etheses.whiterose.ac.uk/2781/.

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4

Bjelic, Sinisa. "Molecular Simulation of Enzyme Catalysis and Inhibition." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-7468.

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5

Lopez, Murielle. "The Effect of Hydration on Enzyme Activity and Dynamics." The University of Waikato, 2008. http://hdl.handle.net/10289/2360.

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Water has long been assumed to be essential for biological function. To understand the molecular basis of the role of water in protein function, several studies have established a correlation between enzyme activity and hydration level. While a threshold of hydration of 0.2 h (grams of water per gram of dried protein) is usually accepted for the onset of enzyme activity, recent works show that enzyme activity is possible at water contents as low as 0.03 h (Lind et al., 2004). Diffusion limitation in these experiments was avoided by monitoring enzyme-catalyzed hydrolysis of gas-phase esters. Ho

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6

Hoeven, Robin. "Investigating the contribution of protein dynamics to catalysis in protochlorophyllide oxidoreductase." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/investigating-the-contribution-of-protein-dynamics-to-catalysis-in-protochlorophyllide-oxidoreductase(029dda21-023f-4fdb-a980-26db7eab4833).html.

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Enzyme dynamics has been established to play a crucial role in catalysis, and it has therefore become an important area of research to better understand enzymatic rate enhancements. The light-activated enzyme protochlorophyllide oxidoreductase (POR) is a well-studied model system where dynamics are known to be important for catalysis. The catalytic reaction involves a sequential hydride and proton transfer to reduce the C17-C18 double bond in the protochlorophyllide (Pchlide) substrate with NADPH as a cofactor to yield the chlorophyllide (Chlide) product. Both H-transfer steps are established

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7

Stojkovic, Vanja. "Contribution of active site dynamics to enzyme catalysis: study on a series of mutants of dihydrofolate reductase." Diss., University of Iowa, 2012. https://ir.uiowa.edu/etd/5062.

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This thesis describes an effort to expand current knowledge of catalysis in biological systems. The focus is on understanding how enzymes activate covalent bonds and specifically to study C-H bond activation via enzymes. The work presented here examined the role of protein dynamics and hydrogen tunneling in enzyme catalysis. Dihydrofolate reductase from Escherichia coli (ecDHFR), which catalyzes a single hydride transfer reaction, was selected as the model system for these studies. Intrinsic kinetic isotope effects (KIEs) have been shown to be highly sensitive probes in examining the chemical

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8

Subramaniam, Srisunder. "Studies of conformational changes and dynamics accompanying substrate recognition, allostery and catalysis in bacteriophage lambda integrase." The Ohio State University, 2005. http://rave.ohiolink.edu/etdc/view?acc_num=osu1111655332.

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9

Molina, Gustavo Avelar. "Caracterização biofísica da dinâmica catalítica de uma xilanase GH11." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/59/59138/tde-17042016-155242/.

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A dinâmica estrutural fundamentando a função das xilanases GH11 ainda não está clara. Novo conhecimento sobre a dinâmica catalítica dessas enzimas é crucial para a engenharia de novas enzimas melhoradas beneficiando, assim, diversas indústrias biotecnológicas e de química verde. Com base nesse fato, esse trabalho teve por objetivo obter novas informações acerca da dinâmica catalítica de uma xilanase GH11, através do uso de um conjunto de diversas técnicas avançadas de biofísica molecular em nível bulk e em nível de molécula única (inglês single molecule ou sm). Para isso, foram projetadas xil

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10

Mills, Landon C. "IMPACT OF CONFORMATIONAL CHANGE, SOLVATION ENVIRONMENT, AND POST-TRANSLATIONAL MODIFICATION ON DESULFURIZATION ENZYME 2'-HYDROXYBIPHENYL-2-SULFINATE DESULFINASE (DSZB) STABILITY AND ACTIVITY." UKnowledge, 2019. https://uknowledge.uky.edu/cme_etds/105.

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Naturally occurring enzymatic pathways enable highly specific, rapid thiophenic sulfur cleavage occurring at ambient temperature and pressure, which may be harnessed for the desulfurization of petroleum-based fuel. One pathway found in bacteria is a four-step catabolic pathway (the 4S pathway) converting dibenzothiophene (DBT), a common crude oil contaminant, into 2-hydroxybiphenyl (HBP) without disrupting the carbon-carbon bonds. 2’-Hydroxybiphenyl-2-sulfinate desulfinase (DszB), the rate-limiting enzyme in the enzyme cascade, is capable of selectively cleaving carbon-sulfur bonds. Accordingl

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11

Silva, Mojica Ernesto. "Polymer-silica Hybrids for Separation of CO2 and Catalysis of Organic Reactions." University of Akron / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=akron1398439043.

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12

Danielsson, Jonas. "Computational chemistry studies of UV induced processes in human skin." Doctoral thesis, Stockholm : Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi, Univ, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-261.

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13

Born, Benjamin [Verfasser]. "Terahertz spectroscopy of proteins : hydration dynamics of proteins during folding, enzyme catalysis and in chemical equilibrium / Benjamin Philipp Born." 2010. http://d-nb.info/1007559586/34.

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14

Ergel, Burce. "The Catalytic Efficiency and Conformational Dynamics of Escherichia coli DNA Repair Enzyme AlkB." Thesis, 2012. https://doi.org/10.7916/D84178PJ.

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Enzymes catalyze specific reactions in almost all cellular processes, including DNA replication and repair, transcription, translation, signal transduction and energy production. Therefore, extensive efforts are underway to understand the functions and mechanisms of these processes. The potential contribution of the conformational dynamics of enzymes to their high catalytic power has received particular attention in the last decades. Studies indicate that protein dynamics are involved in substrate binding and product release; however, the role of dynamics in catalysis is still controversial. H

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15

Wu, Zheng-Qian, and 吳政謙. "Study of Non-Linear Dynamics in an Enzyme Catalysis System Involving Substrate Activation." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/58604616939664172888.

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碩士<br>國立聯合大學<br>化學工程學系碩士班<br>100<br>The interesting non-linear dynamical behaviors exhibited in certain chemical reaction systems, such as multiple steady states, undamped oscillation, chaos, and so on, often result from unstable steady states. A biochemical system is studied, which involves four enzyme and one substrate in a continuous flow system and is used to discuss dynamical behaviors of the derived chemical reaction networks. Suppose components of isothermal reactions obey the mass action law and their dynamical behaviors can be described by the system of non-linear ordinary differentia

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16

McGowan, Lauren. "Using Molecular Dynamics to Elucidate the Mechanism of Cyclophilin." 2014. http://scholarworks.gsu.edu/chemistry_diss/88.

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Cyclophilins are ubiquitous enzymes that are involved in protein folding, signal transduction, viral proliferation, oncogenesis, and regulation of the immune system. Cyclophilin A is the prototype of the cyclophilin family. We use molecular dynamics to describe the catalytic mechanism of cyclophilin A in full atomistic detail by sampling critical points along the reaction coordinate, and use accelerated molecular dynamics to sample cis-trans interconversions. At these critical points, we analyze the conformational space sampled by the active site, flexibility of the enzyme backbone, and modula

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17

Genodepa, Jerome G. "Digestive enzyme dynamics during early life stages of the mud crab, Scylla serrata and the spiny lobster, Panulirus ornatus." Thesis, 2015. https://researchonline.jcu.edu.au/46242/1/46242-genodepa-2015-thesis.pdf.

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The mud crab, Scylla serrata and the spiny lobster, Panulirus ornatus, are high value crustaceans in the tropics and sub-tropics of the Indo-Pacific region subject to intense fisheries pressure, particularly in Asia where no catch limits are imposed and fishery laws are often not strictly enforced. Because of increasing demand and dwindling fisheries landings, interest in aquaculture of both species has grown strongly over recent years. However, continued dependence on wild seed for stocking has been a major bottleneck for expansion and further development of aquaculture industries for both sp

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