Relevant bibliographies by topics / CAMP induced conformational changes

Academic literature on the topic 'CAMP induced conformational changes'

Author: Grafiati
Published: 9 March 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'CAMP induced conformational changes.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "CAMP induced conformational changes"

1

Introini, Bianca, Andrea Saponaro, Alessio Bonucci, Oliver Rauh, Francesca Cantini, Lucia Banci, Gerhard Thiel, and Anna Moroni. "Camp-Induced Conformational Changes in the C-Linker of HCN4." Biophysical Journal 118, no. 3 (February 2020): 419a. http://dx.doi.org/10.1016/j.bpj.2019.11.2365.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Baichoo, Noel, and Tomasz Heyduk. "Mapping Conformational Changes in a Protein: Application of a Protein Footprinting Technique to cAMP-Induced Conformational Changes in cAMP Receptor Protein†." Biochemistry 36, no. 36 (September 1997): 10830–36. http://dx.doi.org/10.1021/bi970714v.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Hinds, M. G., R. W. King, and J. Feeney. "19F n.m.r. studies of conformational changes accompanying cyclic AMP binding to 3-fluorophenylalanine-containing cyclic AMP receptor protein from Escherichia coli." Biochemical Journal 287, no. 2 (October 15, 1992): 627–32. http://dx.doi.org/10.1042/bj2870627.

Full text
Abstract:
A fluorine-containing analogue of the cyclic AMP (cAMP) receptor protein (CRP) from Escherichia coli was prepared by biosynthetic incorporation of 3-fluorophenylalanine (3-F-Phe). 19F n.m.r. studies on this protein have provided direct evidence for cAMP-induced conformational changes not only within the cAMP-binding domain but also within the hinge region connecting the cAMP-binding domain to the DNA-binding headpiece. At 313 K, the 19F n.m.r. spectrum of [3-F-Phe]CRP showed five signals corresponding to the five phenylalanine residues as expected for a symmetrical dimer. Proteolysis of [3-F-Phe]CRP with subtilisin produced a fragment (the alpha-fragment) containing the cAMP-binding domain. The alpha-fragment contains all the phenylalanines except for Phe-136, a residue located in the hinge region. By comparing the 19F spectra of [3-F-Phe]CRP and its alpha-fragment, the signal for Phe-136 was assigned. The chemical shifts of the corresponding signals in the two spectra are similar, indicating that the alpha-fragment retains the structure it has in the intact protein. The largest cAMP-induced shift was observed for the signal from Phe-136 providing direct evidence for a conformational change in the hinge region. However, whereas binding of a single cAMP molecule to a CRP dimer is known to be sufficient to activate the DNA binding, the n.m.r. data indicate that the hinge region does not have the same conformation in both subunits when only one cAMP molecule is bound.
APA, Harvard, Vancouver, ISO, and other styles
4

Cheng, Xiaodong, Shmuel Shaltiel, and Susan S. Taylor. "Mapping Substrate-Induced Conformational Changes in cAMP-Dependent Protein Kinase by Protein Footprinting†." Biochemistry 37, no. 40 (October 1998): 14005–13. http://dx.doi.org/10.1021/bi981057p.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Introini, Bianca, Andrea Saponaro, Alessio Bonucci, Oliver Rauh, Francesca Cantini, Lucia Banci, Gerhard Thiel, and Anna Moroni. "Chimeric HCN Channels for Studying Camp-Induced Conformational Changes in the C-Linker." Biophysical Journal 116, no. 3 (February 2019): 301a. http://dx.doi.org/10.1016/j.bpj.2018.11.1631.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Prade, Lars, Richard A. Engh, Andreas Girod, Volker Kinzel, Robert Huber, and Dirk Bossemeyer. "Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential." Structure 5, no. 12 (December 1997): 1627–37. http://dx.doi.org/10.1016/s0969-2126(97)00310-9.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Tworzydło, Magdalena, Agnieszka Polit, Jan Mikołajczak, and Zygmunt Wasylewski. "Fluorescence quenching and kinetic studies of conformational changes induced by DNA and cAMP binding to cAMP receptor protein from Escherichia coli." FEBS Journal 272, no. 5 (February 17, 2005): 1103–16. http://dx.doi.org/10.1111/j.1742-4658.2005.04540.x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Fic, Ewelina, Agnieszka Polit, and Zygmunt Wasylewski. "Kinetic and Structural Studies of the Allosteric Conformational Changes Induced by Binding of cAMP to the cAMP Receptor Protein fromEscherichia coli†." Biochemistry 45, no. 2 (January 2006): 373–80. http://dx.doi.org/10.1021/bi051586a.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

López, Ximena, Rosalba Escamilla, Paola Fernández, Yorley Duarte, Fernando González-Nilo, Nicolás Palacios-Prado, Agustín D. Martinez, and Juan C. Sáez. "Stretch-Induced Activation of Pannexin 1 Channels Can Be Prevented by PKA-Dependent Phosphorylation." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9180. http://dx.doi.org/10.3390/ijms21239180.

Full text
Abstract:
Pannexin 1 channels located in the cell membrane are permeable to ions, metabolites, and signaling molecules. While the activity of these channels is known to be modulated by phosphorylation on T198, T308, and S206, the possible involvement of other putative phosphorylation sites remains unknown. Here, we describe that the activity of Panx1 channels induced by mechanical stretch is reduced by adenosine via a PKA-dependent pathway. The mechanical stretch-induced activity—measured by changes in DAPI uptake—of Panx1 channels expressed in HeLa cell transfectants was inhibited by adenosine or cAMP analogs that permeate the cell membrane. Moreover, inhibition of PKA but not PKC, p38 MAPK, Akt, or PKG prevented the effects of cAMP analogs, suggesting the involvement of Panx1 phosphorylation by PKA. Accordingly, alanine substitution of T302 or S328, two putative PKA phosphorylation sites, prevented the inhibitory effect of cAMP analogs. Moreover, phosphomimetic mutation of either T302 or S328 to aspartate prevented the mechanical stretch-induced activation of Panx1 channels. A molecular dynamics simulation revealed that T302 and S328 are located in the water–lipid interphase near the lateral tunnel of the intracellular region, suggesting that their phosphorylation could promote conformational changes in lateral tunnels. Thus, Panx1 phosphorylation via PKA could be modulated by G protein-coupled receptors associated with the Gs subunit.
APA, Harvard, Vancouver, ISO, and other styles
10

Buechler, Joseph A., Thomas A. Vedvick, and Susan S. Taylor. "Differential labeling of the catalytic subunit of cAMP-dependent protein kinase with acetic anhydride: substrate-induced conformational changes." Biochemistry 28, no. 7 (April 4, 1989): 3018–24. http://dx.doi.org/10.1021/bi00433a042.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "CAMP induced conformational changes"

1

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 text
Abstract:
Hyperpolarization-activated cyclic nucleotide-gated (HCN1-4) channels are the molecular correlate of Ih (or If) current, which plays a key role in the control of neuronal and cardiac rhythmicity. HCNs are activated by the hyperpolarization of the membrane potential and further regulated by the direct binding of cyclic AMP (cAMP) to the cytoplasmic Cyclic Nucleotide Binding Domain (CNBD). cAMP binding determines the removal of the autoinhibitory action exerted by the CNBD on the pore opening and causes conformational changes that propagate from the CNBD to the pore through the C-linker, increasing channel open probability and speeding activation kinetics. cAMP modulation of HCN controls rhythmicity and excitability at cardiac and neuronal level and pain perception. Thus, in order to understand several physiological functions, as well as diseases affecting both the cardiac and neuronal system, a detailed description of the cAMP-induced conformational changes is required. Moreover, functional studies indicate that cAMP binding to the CNBD induces the transition of the C-terminal domains, from dimer of dimer to tetramer and that this transition is driven by the movements of the C-linker. The goal of this work is to describe the propagation of the movements through the C-linker to the pore. To this end, I have applied spectroscopic techniques, such as Electron Paramagnetic Resonance (EPR) and Double Electron-Electron Resonance (DEER) to study dynamic changes in the structure of the purified and labelled protein. First, I constructed a chimeric channel by fusing the C-linker/CNBD of human HCN4 to the prokaryotic pore domain of KcsA. This protein has the advantage that can be produced and easily purified in E. coli. Isothermal Titration Calorimetry (ITC) and Differential Scanning Calorimetry (DSC) measurements demonstrated that the purified chimera is able to bind cAMP. Particularly, ITC gave a Kd value of 1.7 μM, which agrees with the one previously published for the isolated C-linker/CNBD fragment of HCN4. Moreover, the rescue of a K+-uptake deficient E. coli strain demonstrated that the chimeric channel is able to conduct a K+ ions flow. EPR-DEER experiments performed on the chimera revealed that the binding of cAMP to the CNBD domain causes clear conformational changes in the C-terminal region, which transits from a dimer of dimers conformation to a 4-fold symmetrical gating ring. These data confirm previous biochemical and functional indication obtained on the full-length channel and give further details on the direction and the extent of subunit displacement occurring during the conformational transition. The transition of the channel from a dimer of dimer to a tetrameric configuration of the cytosolic domain might reflect a pre-conditioning state for cAMP action on channel gating and partly explains the agonist activity exerted by cAMP on channel kinetics and open probability.
APA, Harvard, Vancouver, ISO, and other styles
2

Liu, 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 text
Abstract:
Spectrofluorimetry is utilized as a novel real time non-invasive optical assay to investigate whether the exposure of bovine serum albumin (BSA) to extremely low frequency (ELF) and radio frequency (RF) electromagnetic (EM) fields causes conformational changes in the protein distinct from those due to heating alone. Such conformational changes would alter the protein's fluorescence spectrum, and could indicate a potential for EM induced altered biological activity of proteins in-vivo. The development of both the ELF and RF exposure system are described, discussed and evaluated. Since ELF electric fields do not exhibit propagation phenomena within the dimensions of the apparatus, a quasi-static approach is taken and a stainless steel parallel-plate exposure system is designed in a cuvette. While at RF, FDTD software is employed to facilitate a TEM cell based exposure system evaluation and optimization, and also to provide preliminary SAR distributions in the BSA sample as a control for future experimental measurements. The sensitivity of the systemic methodology (including the statistical analysis method) is demonstrated, indicating that the system is capable of detecting fluorescence changes as small as 0.032%. At ELF, the effects of six different high field strength 100Hz EM exposure paradigms at different temperatures on BSA conformational changes are presented and critically discussed. While at RF, four different 430MHz exposure paradigms are applied, with either intermittent or continuous bursts of TETRA or CW signals, at different average SAR levels. Statistical tests are used to analyse the experimental data. Periodical fluorescence oscillations are observed under both ELF and RF exposures, but their origins are considered to be convection currents due to unevenly distributed energy injections into the solution.
APA, Harvard, Vancouver, ISO, and other styles
3

Wolter, 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 text
APA, Harvard, Vancouver, ISO, and other styles
4

Hedley, 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 text
Abstract:
G-protein coupled receptors (GPCRs) are one of the main targets for drug design. GPCR pharmaceutical research has bottlenecked on drug research, and the current assay systems are not creating therapeutic drugs from drug hits. The principal aim of this project was to establish a relationship between drug affinity (PKi) and drug intrinsic efficacy (Emax) using receptor conformational change parameters (measurements defined by fluorescence resonance energy transfer (FRET) experiments) to provide a new way of screening for the intrinsic efficacy of a drug. This project aimed to develop a drug screen based on the hypothesis that ligand intrinsic efficacy was linked to ligand induced receptor conformational change. Using FRET technology, the extent and rate of ligand induced receptor conformational changes were investigated. In contrast to the clear cut nature of ligand intrinsic efficacy and the extent of ligand induced receptor conformational change observed in the literature no correlation was found in this project on the FRET reporter construct A2A.4C.CFP. FRET studies revealed some key findings into the receptor activation mechanisms of the A2aR. Firstly, that different agoinsts induce different conformational states of the receptor and at different rates, thus these finding support activation models proposed by Koshland and are inline with work carried out by Kobilka. Secondly, that different agonists imposed different conformational restrictions/conditions on the resultant conformation of the second agonist applied. This finding opens up the possibility for drug design, as it is possible that the resultant conformation of a drug applied after the receptor has been activated by a previously applied agonist may result in a different pharmacological response, and hence may open up new avenues for investigation. cAMP functional studies were carried out to classify and rank the intrinsic efficacy of the test ligands and to assess effects of the mutations within the A2A.4C.CFP receptor on downstream signalling. All the ligands tested with the exception of compound 15 were reported to be full A2aR agonists in the literature. However compounds CV 1808 and 2Chloroadenosine both generated only partial responses in this assay. This finding may be reflective of differences in receptor activation mechanism of these two compounds compared to the other full agonists.
APA, Harvard, Vancouver, ISO, and other styles
5

Gao, 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 text
APA, Harvard, Vancouver, ISO, and other styles
6

Hörsch, 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 text
APA, Harvard, Vancouver, ISO, and other styles
7

Fotheringham, 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 text
Abstract:
Approximately 50 % of current pharmaceutical drugs target the G protein-coupled receptor (GPCR) family, rendering an understanding of the mechanisms behind their actions critical. Dopamine is a key neurotransmitter involved in motor function and behaviour and has been associated with disorders such as Parkinson's disease and schizophrenia. Within the present study, a Fluorescence Resonance Energy Transfer (FRET)-based conformational change sensor was created to study dopamine D2S receptor responses to ligands to gain an understanding of the mechanisms underlying ligand-induced activation. Chimaeric receptors were created with a tetracysteine sequence FlAsH binding motif at varying positions within intracellular loop 3 and CFP fused to the C-terrninal where FlAsH and CFP formed a convenient FRET pair. The constructs were transiently transfected into HEK293 cells and characterised using confocal and FRET microscopy. The 353-CFP-D2s receptor was well expressed at the cell surface and produced agonist-induced FRET changes and therefore was used to create a stably expressing HEK293 cell line. Radioligand binding and eSS]GTPyS binding assays showed that the 353-CFP-D2s receptor had a pharmacological profile similar to the native D2S receptor. On application of agonist (NP A, dopamine, m-tyramine, p- tyramine and (- )-3-PPP) to the 353-CFP-D2s receptor, a concentration dependent decrease in FRET was detected which was completely reversed when agonist was removed. The extent of FRET response was found to broadly correlate with the extent of G protein activation. The forward rate constant of the FRET change was also found to alter in an agonist-concentration dependent manner while the reverse rate was concentration independent. Throughout the project, the control and optimisation of experimental variables was found to be crucial for successful use of this FRET -based system. In conclusion, this sensor and the use of this technique could be very useful to aid understanding of activation of this important GPCR. 111.
APA, Harvard, Vancouver, ISO, and other styles
8

Gan, 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 text
Abstract:
This thesis concentrates on the study of DNA structures by X-ray crystallography. The first chapter introduces the molecules under study; whilst chapter two describes the theories and methodologies that are closely involved. The following three chapters contain the main results and describe eight refined structures. Chapter three examines ion influences upon an unusual non-planar G/C quadruplex formed by the heptamer nucleotide d(GCATGCT), in which the highly carcinogenic element nickel has be.en found to cause dramatic distortions in this otherwise very stable DNA structure: Chapter four is focused on the DNA-intercalator complexes formed between the hexamer nucleotide d(CGTACG) and two bis-acridine derivatives that differ at their linkers in terms of length and charge. It was found that the bis-acridine compound with a linker consisting of a nitrogen plus six carbon atoms was able to crosslink the DNA m~lecules in a novel wa.y, in which the acridine chromophore is rotated around its plane normal by 1800 away from the conformation found previously in the monomers and one side-chain attached bis-acridine derivatives. In the complex of the same oligonucleotide and another bis-acridine' derivative with a longer linker in the presence of C02 +, the best electron density around the ligand, compared with all the other reported analogues, was obtained from the in-house diffractometer. Chapter five describes two A-DNA structures formed by the same sequences that are crystallised in different spacegroups. The novel choice of the sequences was inspired by a recent publication reporting a statistical analysis of recombination sequences in the human genome. The chosen decamer nucleotide contains the recombination hotspot heptamer CCTCCCT. ., Chapter six presents the results of G-quadruplex crystallisation studies, and some preliminary X-ray diffraction data. Chapter seven, as the last chapter of the thesis, , lists the ongoing projects and describes future work.
APA, Harvard, Vancouver, ISO, and other styles
9

Saba, 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 text
APA, Harvard, Vancouver, ISO, and other styles
10

Schein, 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 text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "CAMP induced conformational changes"

1

Steitz, T. A., R. Harrison, I. T. Weber, and M. Leahy. "Ligand-Induced Conformational Changes in Proteins." In Ciba Foundation Symposium 93 - Mobility and Function in Proteins and Nucleic Acids, 25–46. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720752.ch3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Drochioiu, Gabi. "Silver-Induced Conformational Changes of Polypeptides." In Encyclopedia of Metalloproteins, 2063–71. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_576.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Irie, Masahiro. "Light-Induced Conformational Changes of Synthetic Polymers." In Photophysical and Photochemical Tools in Polymer Science, 269–91. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4726-9_12.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Herberg, Friedrich W., and Susan S. Taylor. "Conformational and Shape Changes Associated with cAMP- Dependent Protein Kinase." In Cellular Regulation by Protein Phosphorylation, 119–23. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75142-4_14.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Brautigam, Chad A., Catherine A. Wakeman, and Wade C. Winkler. "Methods for Analysis of Ligand-Induced RNA Conformational Changes." In Methods in Molecular Biology, 77–95. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-558-9_7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Allegretto, Elizabeth A. "Ligand-Induced Conformational Changes in Estrogen Receptors-α and -β." In Selective Estrogen Receptor Modulators, 19–28. Totowa, NJ: Humana Press, 2002. http://dx.doi.org/10.1007/978-1-59259-157-2_2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Andréasson, Ulf, and Lars Erik Andréasson. "Time-Resolved, Light-Induced Conformational Changes in R. sphaeroides Reaction Centers." In Photosynthesis: Mechanisms and Effects, 791–93. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_186.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Brändén, Carl-Ivar, and Hans Eklund. "Coenzyme-Induced Conformational Changes and Substrate Binding in Liver Alcohol Dehydrogenase." In Novartis Foundation Symposia, 63–80. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720424.ch5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Irie, Masahiro. "Light-Induced Conformational Changes of Polymers in Solution and Gel Phase." In ACS Symposium Series, 107–22. Washington, DC: American Chemical Society, 1987. http://dx.doi.org/10.1021/bk-1987-0358.ch010.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Weibezahn, Karl F., Gudrun Knedlitschek, Werner Sontag, Johannes C. Stein, Eric Gottwald, and Hermann Dertinger. "Changes of Intercellular Communication Induced by Alternating Electric Fields Correlate with Changes of cAMP." In Electricity and Magnetism in Biology and Medicine, 445–47. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4867-6_104.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "CAMP induced conformational changes"

1

Spuhler, Philipp S., Jelena Knezevic, Ayca Yalcin, Peter Droge, Ulrich Rant, and M. Selim Unlu. "Real-time kinetics measurements of protein induced conformational changes in DNA." In LEOS 2009 -22nd Annuall Meeting of the IEEE Lasers and Electro-Optics Society. LEO 2009. IEEE, 2009. http://dx.doi.org/10.1109/leos.2009.5343144.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Liu, W., G. G. Cook, A. T. Barker, and L. A. Coulton. "Investigation of EMF induced protein conformational changes using an optical assay." In Propagation Conference (LAPC). IEEE, 2008. http://dx.doi.org/10.1109/lapc.2008.4516893.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Kaazempur-Mofrad, Mohammad R., Peter J. Mack, Helene Karcher, Javad Golji, and Roger G. Kamm. "Stress-Induced Mechanotransduction: Some Preliminaries." In ASME 2003 International Mechanical Engineering Congress and Exposition. ASMEDC, 2003. http://dx.doi.org/10.1115/imece2003-43215.

Full text
Abstract:
Mechanical stimuli affect nearly every aspect of cellular function, yet the underlying mechanisms of transduction of force into biochemical signals are not clearly understood. One hypothesis is that forces transmitted via individual proteins, either at the site of cell adhesion to its surroundings or within the stress-bearing members of the cytoskeleton, cause conformational changes that change their binding affinity to other intracellular molecules. This altered equilibrium state can subsequently initiate biochemical signaling cascades of produce immediate structural changes. This paper addresses the distribution of forces within the cell resulting from specific mechanical stimuli, computed using a 3-D multi compartment, continuum, viscoelastic finite element model, and uses these to estimate the forces transmitted by individual proteins and protein complexes. These levels of force are compared to those known to produce conformational changes in cytoskeletal proteins, as speculated from magnetocytometry observations and computed by molecular dynamics.
APA, Harvard, Vancouver, ISO, and other styles
4

Chakrabarti, Bireswar, Krishnagopal Mandal, Stephen N. Joffe, and John A. Parrish. "Light-Induced Conformational Changes Of Lens Proteins: Photochemistry And Photophysics Of The Process." In Cambridge Symposium-Fiber/LASE '86. SPIE, 1987. http://dx.doi.org/10.1117/12.937333.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Giliberti, V., R. Polito, E. Ritter, A. Nucara, P. Calvani, M. Broser, P. Hegemann, et al. "Light-induced conformational changes of protein receptors probed by difference mid-IR microspectroscopy." In 2018 43rd International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz 2018). IEEE, 2018. http://dx.doi.org/10.1109/irmmw-thz.2018.8510076.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Nara, Masayuki, Masaru Tanokura, and Mitsuo Tasumi. "Fourier transform infrared studies on conformational changes of calmodulin induced by metal-ion binding." In Fourier Transform Spectroscopy: Ninth International Conference, edited by John E. Bertie and Hal Wieser. SPIE, 1994. http://dx.doi.org/10.1117/12.166602.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Lamichhane, Tika Ram, and Hari Prasad Lamichhane. "Thiocyanate-induced conformational changes in thyroid hormone receptor-β by model ligand-T2SCN interactions." In PROCEEDINGS OF THE 14TH ASIA-PACIFIC PHYSICS CONFERENCE. AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0037068.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Avadanei, Mihaela, and Gheorghe Fundueanu. "ATR-FTIR spectroscopic studies of thermally induced conformational changes of PNIPAAm copolymers in solution." In International Conference on Applications of Optics and Photonics, edited by Manuel F. Costa. SPIE, 2011. http://dx.doi.org/10.1117/12.894398.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Spuhler, Philipp S., Jelena Knezevic, Ayca Yalcin, Peter Droge, Ulrich Rant, and M. Selim Unlu. "A platform for in situ real-time measurement of protein induced conformational changes of DNA." In LEOS 2009 -22nd Annuall Meeting of the IEEE Lasers and Electro-Optics Society. LEO 2009. IEEE, 2009. http://dx.doi.org/10.1109/leos.2009.5343182.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Zhuang, Jie, Juergen F. Kolb, Yu Jing, and Barbara Y. Hargrave. "Pulsed electric field induced conformational changes of mammalian cells revealed by time domain dielectric spectroscopy." In 2012 IEEE 39th International Conference on Plasma Sciences (ICOPS). IEEE, 2012. http://dx.doi.org/10.1109/plasma.2012.6383516.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'CAMP induced conformational changes' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography