Dissertations / Theses on the topic 'CAMP induced conformational changes'
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INTROINI, BIANCA. "DESIGN OF CHIMERIC ION CHANNELS TO MONITOR CAMP-INDUCED CONFORMATIONAL CHANGES AND DYNAMICS." Doctoral thesis, Università degli Studi di Milano, 2020. http://hdl.handle.net/2434/719688.
Full textLiu, Wenchao. "Investigation of electromagnetic field induced protein conformational changes using spectrofluorimetry." Thesis, University of Sheffield, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.574553.
Full textWolter, Tino [Verfasser], and M. [Akademischer Betreuer] Elstner. "Light-induced conformational changes in proteins / Tino Wolter. Betreuer: M. Elstner." Karlsruhe : KIT-Bibliothek, 2013. http://d-nb.info/1046888870/34.
Full textHedley, Diana. "Investigating agonist induced receptor conformational changes on the adenosine A2a receptor." Thesis, University of Reading, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.553235.
Full textGao, Meimei. "Reversibility of anesthetic-induced conformational and functional changes in the purple membrane." Thèse, Trois-Rivières : Université du Québec à Trois-Rivières, 2004. http://www.uqtr.ca/biblio/notice/resume/18186324R.pdf.
Full textHörsch, Daniel [Verfasser]. "Monitoring light induced conformational changes in photoreceptors by time resolved spectroscopy / Daniel Hörsch." Berlin : Freie Universität Berlin, 2009. http://d-nb.info/1023623048/34.
Full textFotheringham, Helen L. "Investigation of ligand-induced conformational changes of the dopamine D2s receptor using fluorescence resonance energy transfer." Thesis, University of Reading, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.558734.
Full textGan, Yu. "X-ray crystallographic studies of DNA structures : conformational changes induced by metal cations, organic ligands and sequence variation." Thesis, University of Reading, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.487234.
Full textSaba, Rami. "A contribution to the study of the bovine heart Na/Ca exchanger membrane topology and of the conformational changes induced by regulatory ligands binding." Doctoral thesis, Universite Libre de Bruxelles, 2000. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/211796.
Full textSchein, Peter Christian [Verfasser]. "Proteomic identification of posttranslational modifications: cAMP-induced changes of phosphorylation and investigation of novel approaches detecting posttranslational modifications at lysine and arginine residues / Peter Christian Schein." Bonn : Universitäts- und Landesbibliothek Bonn, 2020. http://d-nb.info/1208937456/34.
Full textMalloni, Wilhelm Massimiliano [Verfasser], and Hans Robert [Akademischer Betreuer] Kalbitzer. "AUREMOL-QTA, a program package for NMR based automated recognition and characterization of local and global conformational changes in proteins induced by ligand binding as external perturbation / Wilhelm Massimiliano Malloni. Betreuer: Hans Robert Kalbitzer." Regensburg : Universitätsbibliothek Regensburg, 2011. http://d-nb.info/1030178836/34.
Full textGuerriero, Andrew. "Variable pressure NMR analyses to assess compressive motion in PETNR and catalytically germane PETNR:Ligand complexes." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/variable-pressure-nmr-analyses-to-assess-compressive-motion-in-petnr-and-catalytically-germane-petnrligand-complexes(f9d8a882-b05b-47ac-86c4-3987c78e5494).html.
Full textYang, Hsin Yi, and 楊欣奕. "Substrate-induced conformational changes in ArsA protein." Thesis, 1994. http://ndltd.ncl.edu.tw/handle/08399571986983481911.
Full text國立中山大學
生命科學研究所
82
ArsA蛋白質是陰離子傳輸系統的催化次單元,在其陰離子受質存在下,才 具備ATP水解的活性。先前研究顯示ArsA蛋白質的ATP接合部位與陰離子接 合部位有交互作用。以五種蛋白質水解酵素限制性的切除反應來偵測 ArsA蛋白質經受質ATP、鎂離子與陰離子等引發的結構變化時,trypsin的 切除反應確認了ATP與陰離子接合部位有交互作用,而elastase及 chymotrypsin A4切除反應則顯示了ATP接合部位與鎂離子接合部位有交互 作用。另受質和ArsA蛋白質接合的順序不同亦會造成ArsA蛋白質不同的結 構變化,其中加入ATP再加入陰離子與加入陰離子後再加入ATP,以 trypsin切除反應分析時,顯示後者多出一56kDa的產物。另外,63kDa ArsA蛋白質經trypsin水解後的61kDa與30kDa產物均不具催化活性,也失 去和Red Agarose接合的特性,但仍可與陰離子接合,此顯示被切去的 2kDa片段在ATP的接合及催化活性上扮演重要的角色,而陰離子接合部位 即位於此30kDa片段上。
Voß, Béla. "Conformational Changes in Ligand Binding Processes." Doctoral thesis, 2015. http://hdl.handle.net/11858/00-1735-0000-0022-5EE0-6.
Full textChen, Chia-Yi, and 陳佳儀. "Divalent cation-induced conformational changes and oligomerization of KChIP1." Thesis, 2003. http://ndltd.ncl.edu.tw/handle/18463816663669345440.
Full text國立中山大學
生物醫學科學研究所
91
Abstract KChIPs are Kv channel-interacting proteins that bind to the cytoplasmic N-terminus of Kv4 ��-subunits and regulate the ion-current of Kv channel. Several isomeric KChIPs arise from alternative splicing have been identified. These KChIPs share a high degree of sequence homology at their C-terminal region which is constituted with four EF hands, but their N-terminus sequence is notably diversified. Among them, KChIP3/Calseniline/Dream has been found to be a multifunctional protein, and interacts with different targets according to its cellular sub-localization. Noticeably, KChIP3 shows a Ca2+-dependent DNA-binding and oligomerization. In the present study, using 5’-RACE PCR, the KChIP 1 and KChIP2 were successfully amplified from human brain and heart cDNA libraries, respectively. The recombinant KChIP proteins were prepared from E. coli expression system, and purified by His-bind resin or GST-resin according to their fusing proteins. The interaction between the KChIP proteins with divalent cations (Mg2+, Ca2+, Sr2+ and Ba2+) was explored by 8-anilinonaphthalene sulfonate (ANS) fluorescence. The results showed that KChIPs possessed both high affinity and low affinity Ca2+-binding sites. However, only one kind of binding-affinity for the other divalent cations was noted. Removal of EF hand 4 caused an abolishment of the high Ca2+-affinity, and the resulting mutated protein exhibited a similar binding affinity for Ca2+, Mg2+, Sr2+ and Ba2+. The mutant lacked EF hands 3 and 4 lost its ANS-binding ability, but it still could bind with Ca2+. Moreover, this mutated KChIP showed a noticeable change in its secondary structure as evidenced by CD spectra. The results of in vitro cross-linking indicated that KChIP1 and KChIP2 could form homo-oligomer in a Ca2+-dependent manner. Interestingly, hetero-oligomerization between KChIP1 and KChIP2 was noted as revealed by pull down assay. The N-terminal region was not involved in homo- or hetero-oligomerization of KChIPs. Taken together, our findings suggest that the integrity of EF hand 4 is essential for the high affinity for Ca2+, and both EF hands 3 and 4 are crucial for maintaining the conformation of KChIPs. However, the oligomerization reaction is highly dependent upon the presence of EF hands.
Rahaman, Md Toheder. "Processing induced conformational changes of food proteins in relation to antigenicity." Thesis, 2016. https://vuir.vu.edu.au/32300/.
Full textDeshmukh, Sasmit S. "Light-induced conformational changes in the photosynthetic reaction center from Rhodobacter sphaeroides." Thesis, 2009. http://spectrum.library.concordia.ca/976425/1/MR63275.pdf.
Full textAmadi, Sepan Tariq Hassan. "Structure, dynamics and substrate-induced conformational changes of Escherichia coli multidrug transporter (EmrE)." Diss., 2010. http://etd.library.vanderbilt.edu/available/etd-04192010-162108/.
Full textWANG, YAO-FENG, and 王耀鋒. "Probing the methanol-induced conformational changes of proteins by electrospray ionization mass spectrometry." Thesis, 2003. http://ndltd.ncl.edu.tw/handle/85290097081776949304.
Full text國立東華大學
化學系
91
Electrospray ionization mass spectrometry (ESI-MS) has been widely applied in medical, biochemical, and environmental researches. The utility of ESI lies in its ability to produce multiply charged gaseous ions directly from solution. The methanol induced conformational changes of cytochrome c from several animal cells under acidic conditions were studied. The charge state distributions of proteins that were produced during ESI were used to monitor the conformational transitions. At different methanol concentrations, cytochrome c transforms from folded state (0% methanol) into an intermediate state (30% methanol), a helical denatured state (50% methanol) and a helical denatured protected state (90% methanol). These transitions correlate well with earlier studies by optical methods. Further, hydrogen/deuterium exchange rates of cytochrome c from different animal cells at different methanol concentrations were followed by ESI-MS to probe the subtle changes in protein conformation. Accurate exchange rates were obtained by mixing proteins and monitoring their exchange rates simultaneously. The exchange rates for cytochrome c from horse, bovine and dog were comparable, and indicate that their conformations are similar. The exchange rates for the cytochrome c from rabbit and pigeon were different from those of horse at low methanol concentrations (less than 30% methanol), revealing that their conformations (rabbit and pigeon) differ from the others (horse, bovine and dog).
黃韻潔. "Prediction of continuous B-cell epitopes using protein free energy associated with mutation-induced conformational changes." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/45965712009956631224.
Full text國立交通大學
生醫工程研究所
100
Identification of B-cell epitopes plays an important role in vaccine development. Current prediction algorithms mostly rely on amino acid propensity scales and their variants, the results of which depend on a single antigenic phenotype. That viral sequences undergo continuous genetic changes, promoting the emergence of drug resistant strains, renders current prediction methods impractical. In this study, a novel set of features are proposed based on the protein free energy associated with point-mutated structures. To the best of our knowledge, this is the first attempt in this area to predict continuous B-cell epitopes based on protein free energy. I evaluated the novel features on k-nearest neighbor, support vector machine, and artificial neural network models, and achieved prediction accuracy of 74.3%, 66.1%, and 80.0% respectively. In comparison to current predictors, namely ABCPred, BCPred, and AAP, the energy-based models demonstrated better performance.
Kristinsson, Hordur Gudjon. "Conformational and functional changes of hemoglobin and myosin induced by pH: Functional role in fish quality." 2002. https://scholarworks.umass.edu/dissertations/AAI3039370.
Full textMeyer-Lipp, Kerstin [Verfasser]. "Time resolved measurements of sugar binding induced conformational changes in the melibiose permease from Escherichia coli / von Kerstin Meyer-Lipp." 2008. http://d-nb.info/987243888/34.
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