Relevant bibliographies by topics / Conformation

Academic literature on the topic 'Conformation'

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Published: 4 June 2021
Last updated: 29 July 2024

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Journal articles on the topic "Conformation"

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Pavelčík, František, and Eva Luptáková. "The empirical conformational surface of the co(ethylenediamine) ring." Collection of Czechoslovak Chemical Communications 55, no. 6 (1990): 1427–34. http://dx.doi.org/10.1135/cccc19901427.

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The conformational surface of the Co(en) chelate ring was studied by the method of structural correlation. The reduction of dimensionality of the conformation problem was achieved by employing the pseudorotation concept. The empirical potential surface was obtained by statistical treatment of 743 independent conformations from the Cambridge Structural Database. The theoretical potential surface was obtained by molecular mechanics. The minimal-energy conformation is gauche with the Co atom on the two-fold axis. Conformational flexibility also includes an envelope conformation with the N atom bent out of the plane. The transition between the mirror-image symmetrical conformations can occur by a pseudorotation pathway and is accompanied by increased planarity of the ring. The transition state is an envelope conformation with an out-plane Co atom.
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Cresti, Julianna R., Abramo J. Manfredonia, Christopher E. Bragança, Joseph A. Boscia, Christina M. Hurley, Mary D. Cundiff, and Daniel A. Kraut. "Proteasomal conformation controls unfolding ability." Proceedings of the National Academy of Sciences 118, no. 25 (June 14, 2021): e2101004118. http://dx.doi.org/10.1073/pnas.2101004118.

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The 26S proteasome is the macromolecular machine responsible for the bulk of protein degradation in eukaryotic cells. As it degrades a ubiquitinated protein, the proteasome transitions from a substrate-accepting conformation (s1) to a set of substrate-processing conformations (s3 like), each stabilized by different intramolecular contacts. Tools to study these conformational changes remain limited, and although several interactions have been proposed to be important for stabilizing the proteasome’s various conformations, it has been difficult to test these directly under equilibrium conditions. Here, we describe a conformationally sensitive Förster resonance energy transfer assay, in which fluorescent proteins are fused to Sem1 and Rpn6, which are nearer each other in substrate-processing conformations than in the substrate-accepting conformation. Using this assay, we find that two sets of interactions, one involving Rpn5 and another involving Rpn2, are both important for stabilizing substrate-processing conformations. Mutations that disrupt these interactions both destabilize substrate-processing conformations relative to the substrate-accepting conformation and diminish the proteasome’s ability to successfully unfold and degrade hard-to-unfold substrates, providing a link between the proteasome’s conformational state and its unfolding ability.
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Yaoita, Yasunori, and Koichi Machida. "Conformational Assignments of Thujopsene and Related Compounds." Natural Product Communications 14, no. 9 (September 2019): 1934578X1987893. http://dx.doi.org/10.1177/1934578x19878936.

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Conformational analysis suggests that thujopsene (1) can exist as 2 possible conformations, steroidal and nonsteroidal. The conformation of 1 has been investigated using a NMR spectroscopic method. Analyses of the 1H NMR, ROESY, and long-range 1H-1H COSY spectra indicate that 1 exists in a steroidal conformation. Although the conformations of related compounds 2 and 3 were originally assigned as nonsteroidal, careful reexamination of the published NMR data indicates that both compounds exist in a steroidal conformation.
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Wang, Zhangqian, Jieya Deng, Muhammad Umer, Naureen Anwar, Yidang Wang, XingXing Dong, Hua Xu, Yi He, and Chao Gao. "RHPS4 shifted the conformation ensemble equilibrium of Tel24 by preferentially stabilizing the (3 + 1) hybrid-2 conformation." RSC Advances 12, no. 40 (2022): 26011–15. http://dx.doi.org/10.1039/d2ra03959a.

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Tel24 G-quadruplex can form a conformational ensemble consisting of parallel and (3 + 1) hybrid-2 conformations. RHPS4 preferentially stabilized the hybrid-2 conformation and shifted the conformational ensemble equilibrium.
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Su, Yang, Wei Xia, Jing Li, Thomas Walz, Martin J. Humphries, Dietmar Vestweber, Carlos Cabañas, Chafen Lu, and Timothy A. Springer. "Relating conformation to function in integrin α5β1." Proceedings of the National Academy of Sciences 113, no. 27 (June 17, 2016): E3872—E3881. http://dx.doi.org/10.1073/pnas.1605074113.

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Whether β1 integrin ectodomains visit conformational states similarly to β2 and β3 integrins has not been characterized. Furthermore, despite a wealth of activating and inhibitory antibodies to β1 integrins, the conformational states that these antibodies stabilize, and the relation of these conformations to function, remain incompletely characterized. Using negative-stain electron microscopy, we show that the integrin α5β1 ectodomain adopts extended-closed and extended-open conformations as well as a bent conformation. Antibodies SNAKA51, 8E3, N29, and 9EG7 bind to different domains in the α5 or β1 legs, activate, and stabilize extended ectodomain conformations. Antibodies 12G10 and HUTS-4 bind to the β1 βI domain and hybrid domains, respectively, activate, and stabilize the open headpiece conformation. Antibody TS2/16 binds a similar epitope as 12G10, activates, and appears to stabilize an open βI domain conformation without requiring extension or hybrid domain swing-out. mAb13 and SG/19 bind to the βI domain and βI–hybrid domain interface, respectively, inhibit, and stabilize the closed conformation of the headpiece. The effects of the antibodies on cell adhesion to fibronectin substrates suggest that the extended-open conformation of α5β1 is adhesive and that the extended-closed and bent-closed conformations are nonadhesive. The functional effects and binding sites of antibodies and fibronectin were consistent with their ability in binding to α5β1 on cell surfaces to cross-enhance or inhibit one another by competitive or noncompetitive (allosteric) mechanisms.
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Almahmoud, Suliman, Xiaofang Wang, Jonathan L. Vennerstrom, and Haizhen A. Zhong. "Conformational Studies of Glucose Transporter 1 (GLUT1) as an Anticancer Drug Target." Molecules 24, no. 11 (June 7, 2019): 2159. http://dx.doi.org/10.3390/molecules24112159.

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Glucose transporter 1 (GLUT1) is a facilitative glucose transporter overexpressed in various types of tumors; thus, it has been considered as an important target for cancer therapy. GLUT1 works through conformational switching from an outward-open (OOP) to an inward-open (IOP) conformation passing through an occluded conformation. It is critical to determine which conformation is preferred by bound ligands because the success of structure-based drug design depends on the appropriate starting conformation of the target protein. To find out the most favorable GLUT 1 conformation for ligand binding, we ran systemic molecular docking studies for different conformations of GLUT1 using known GLUT1 inhibitors. Our data revealed that the IOP is the preferred conformation and that residues Phe291, Phe379, Glu380, Trp388, and Trp412 may play critical roles in ligand binding to GLUT1. Our data suggests that conformational differences in these five amino acids in the different conformers of GLUT1 may be used to design ligands that inhibit GLUT1.
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Guo, Qing, Yufan He, and H. Peter Lu. "Interrogating the activities of conformational deformed enzyme by single-molecule fluorescence-magnetic tweezers microscopy." Proceedings of the National Academy of Sciences 112, no. 45 (October 28, 2015): 13904–9. http://dx.doi.org/10.1073/pnas.1506405112.

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Characterizing the impact of fluctuating enzyme conformation on enzymatic activity is critical in understanding the structure–function relationship and enzymatic reaction dynamics. Different from studying enzyme conformations under a denaturing condition, it is highly informative to manipulate the conformation of an enzyme under an enzymatic reaction condition while monitoring the real-time enzymatic activity changes simultaneously. By perturbing conformation of horseradish peroxidase (HRP) molecules using our home-developed single-molecule total internal reflection magnetic tweezers, we successfully manipulated the enzymatic conformation and probed the enzymatic activity changes of HRP in a catalyzed H2O2–amplex red reaction. We also observed a significant tolerance of the enzyme activity to the enzyme conformational perturbation. Our results provide a further understanding of the relation between enzyme behavior and enzymatic conformational fluctuation, enzyme–substrate interactions, enzyme–substrate active complex formation, and protein folding–binding interactions.
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Ohhashi, Yumiko, Yoshiki Yamaguchi, Hiroshi Kurahashi, Yuji O. Kamatari, Shinju Sugiyama, Boran Uluca, Timo Piechatzek, et al. "Molecular basis for diversification of yeast prion strain conformation." Proceedings of the National Academy of Sciences 115, no. 10 (February 21, 2018): 2389–94. http://dx.doi.org/10.1073/pnas.1715483115.

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Self-propagating β-sheet–rich fibrillar protein aggregates, amyloid fibers, are often associated with cellular dysfunction and disease. Distinct amyloid conformations dictate different physiological consequences, such as cellular toxicity. However, the origin of the diversity of amyloid conformation remains unknown. Here, we suggest that altered conformational equilibrium in natively disordered monomeric proteins leads to the adaptation of alternate amyloid conformations that have different phenotypic effects. We performed a comprehensive high-resolution structural analysis of Sup35NM, an N-terminal fragment of the Sup35 yeast prion protein, and found that monomeric Sup35NM harbored latent local compact structures despite its overall disordered conformation. When the hidden local microstructures were relaxed by genetic mutations or solvent conditions, Sup35NM adopted a strikingly different amyloid conformation, which redirected chaperone-mediated fiber fragmentation and modulated prion strain phenotypes. Thus, dynamic conformational fluctuations in natively disordered monomeric proteins represent a posttranslational mechanism for diversification of aggregate structures and cellular phenotypes.
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Gaalswyk, Kari, and Christopher N. Rowley. "An explicit-solvent conformation search method using open software." PeerJ 4 (May 31, 2016): e2088. http://dx.doi.org/10.7717/peerj.2088.

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Computer modeling is a popular tool to identify the most-probable conformers of a molecule. Although the solvent can have a large effect on the stability of a conformation, many popular conformational search methods are only capable of describing molecules in the gas phase or with an implicit solvent model. We have developed a work-flow for performing a conformation search on explicitly-solvated molecules using open source software. This method uses replica exchange molecular dynamics (REMD) to sample the conformational states of the molecule efficiently. Cluster analysis is used to identify the most probable conformations from the simulated trajectory. This work-flow was tested on drug molecules α-amanitin and cabergoline to illustrate its capabilities and effectiveness. The preferred conformations of these molecules in gas phase, implicit solvent, and explicit solvent are significantly different.
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Bierzyński, A. "Methods of peptide conformation studies." Acta Biochimica Polonica 48, no. 4 (December 31, 2001): 1091–99. http://dx.doi.org/10.18388/abp.2001_3870.

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In solution most of the peptides assume multiple flexible conformations. Determination of the dominant conformers and evaluation of their populations is the aim of peptide conformation studies, in which theoretical and experimental methods play complementary roles. Molecular dynamics or Monte Carlo methods are quite effective in searching the conformational space accessible to a peptide but they are not able to estimate, precisely enough, the populations of various conformations. Therefore, they must be supplemented by experimental data. In this paper, a short review of the experimental methods, most widely used in peptide conformational studies, is presented. Among them NMR plays the leading role. Valuable information is also obtained from hydrogen exchange, fluorescence resonance energy transfer, and circular dichroism measurements. The advantages and shortcomings of these methods are discussed.
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Dissertations / Theses on the topic "Conformation"

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Ferrari, Marta. "Dynamic conformation : the influence of conformation on equine locomotion." Thesis, Royal Veterinary College (University of London), 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.519518.

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Querolle, Olivier. "Synthèse des taxoïdes à conformation bloquée : vers la conformation active du docetaxel." Paris 11, 2002. http://www.theses.fr/2002PA114831.

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Hogg, John Kirtley. "Conformation of metal chelates." Thesis, University of Bristol, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.259482.

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Link, Justin J. "Ultrafast Protein Conformation Dynamics." The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1230584570.

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Viriyasuthee, Chatavut. "Problem solving by spatial conformation." Thesis, McGill University, 2012. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=107862.

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In computational complexity theory, a reduction is an approach to solving one problemby transforming it into another reference problem in which a solution already exists,thus providing the solution to the original problem in an efficient manner especiallywhen compared with solving the problem directly, which can be costly or even infeasible.The concept of reduction is not only limited to theory; in practice, humansuse past experience to solve problems by \emph{conforming} them, based on analogical reasoning, to known ones that are contained in references or memories.However, because the information retained in references is not always accurate and sometimes filled with redundancies or missing details, the conformation must somehow be robust enough to tolerate these uncertainties.In this thesis, we construct a framework for problem solving by reduction, and we present it in the robotics domain where contexts of problems can be represented using graphical spaces. The process has to match an input problem space to another one in a reference in order to retrieve a solution; we call this process spatial conformation. The content of this thesis can be divided into two parts.First, we develop a general approach and mathematical framework for a range of problem solving challenges to be addressed by reduction. Then we shift our attention to a class of constraint satisfaction problems formulated within the spatial conformation framework. An implementation for each part in robotics applications has been demonstrated to serve as empirical evaluation.
Selon la théorie de la complexité des algorithmes, une réduction est une approche pour résoudre unproblème en le transformant en un autre problème de référence qui a déjà été résolu. Ceci permet de trouver une solution à ce problème initial d'une manière efficace, comparemment à essayer de le résoudre directement, ce qui pourrait être coûteux ou même infaisable. Le concept de réduction n'est pas seulement constrainte à la théorie, en pratique,les humains utilisent leurs expériences pour résoudre de nouveaux problèmes en se basant surleurs raisonnements analogiques et en les conformant aux problémes qui se trouvent dans leurs références ou leurs souvenirs. Cependant, parce que les informations conservées dans les références ne sont pas toujours exactes etparfois manquent des détails, la conformation doit en quelque sorte être suffisamment robuste pour tolérer ces incertitudes. Dans cette thèse, nous construisons un systéme de résolution de problèmes basé sur la méthode de réduction, et nous le présentons dans le domaine de la robotique dans lequel les contextes des problèmes peuvent être représentés dans une espace geométrique. Nous définissons la conformation spatiale par le processus de correspondence entre un probléme d'origine et un autre probléme de référence. Tout d'abord, nous développons une approche générale pour résoudre une série de problèmes devant être traités par réduction. Par la suite, nous mettons l'accent sur une catégorie de problèmes de satisfaction de constraintesformulé dans le système de conformation spatiale. Une implémentation de chaque partie dans les applications de la robotique a été démontrée pour servir d'évaluation empirique.
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Lu, Yanling. "Solution conformation of engineered antibodies." Thesis, University of Nottingham, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.442304.

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Oussaid, Boualem. "Thiophène, pyrrole : synthèse, conformation, macrocycles." Toulouse 3, 1992. http://www.theses.fr/1992TOU30198.

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De nouveaux composes, derives du thiophene ou du pyrrole ont ete synthetises en plusieurs etapes. La conformation de divers composes thiopheniques ou pyrroliques a ete etablie a partir de calculs theoriques, de mesures de moments dipolaires et a partir du couplage stereospecifique a travers cinq liaisons. Quelques macrocycles possedant deux, trois ou quatre restes thiophene ou pyrrole a 18, 20, 30, 34 ou 40 chainons ont ete obtenus par des cyclisations de type 2+2, 3+3 ou 4+4
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Bowers, David J. "Chlorophosphazenes: Synthesis, Structure and Conformation." University of Akron / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=akron1374508951.

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Albiser, Guy. "Etude des conformations et des transitions de forme de l'ADN et des polynucléotides par la diffraction RX de fibres et la modélisation moléculaire." Nancy 1, 1992. http://docnum.univ-lorraine.fr/public/SCD_T_1992_0017_ALBISER.pdf.

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L'ADN et les polynucleotides étirés en fibres orientées sont étudiés par diffraction des rayons X de conditions physico-chimiques modifiables: l'humidité relative environnante, le pourcentage du cation alcalin associé, la fixation de cation métallique et la tension mécanique appliquée. En utilisant les informations obtenues par diffraction RX et des contraintes structurales provenant de résultats spectroscopiques, il est proposé: une discrimination entre modèles conformationnels de la forme b; des modèles conformationnels pour les formes a, b, c de l'ADN et d du poly (da-dt)#2. Une méthode originale, fondée sur les mesures de dimension de fibre, permet d'analyser les transitions a-b et b-c de l'ADN, d- a-b, d-b du poly (da-dt)#2 et z-b du poly (dc-dc)#2. Pour chaque transition, on mesure les variations du nombre de molécules d'eau associées à un nucléotide.
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Florane, H. "Exploring protein conformation with mass spectrometry." Thesis, University of Edinburgh, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.650980.

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The first part of this thesis describes the development and viability of a phase I screening system for obtaining a rank order of affinity of novel ligands against the immunophilin, Cyclophilin A (CypA). The naturally occurring inhibitor Cyclosporin A (CsA) was used as a positive control to validate a method for calculating the dissociation constant (Kd). An HPLC autosampler and pumping system was used as a high throughput on-line electrospray ionisation (ESI)-MS sampling system. Optimised ESI conditions were then used to screen novel ligands from 3 combinatorial libraries and approaches for data analysis is discussed. Hydrogen/deuterium exchange (HDX) can be used directly and indirectly as a means for studying protein conformations. Melittin, the major component of honey bee venom is taken here as a model system for studying secondary structure in solution and the gas phase. Comprising a 26 amino acid polypeptide, melittin occupies a random coil in aqueous conditions which can be transformed into an α-helix under increasingly hydrophobic conditions. A variety of HDX techniques were utilised: i) comparing rats of deuterium (d-) uptake by direct infusion – ESI at different pDs and methanol concentrations; ii) PLIMSTEX (protein-ligand interactions by mass spectrometry, titration and HDX) at high and low salt concentrations with varying pDs; iii) gas phase exchange in an LCQ ion trap using He/d­-methanol as the bath gas. Melittin was pre-incubated in a variety of methanol concentrations. Comparing results from these different approaches, α-helical retention has been shown to exist in the N-terminal half of the peptide. All the afore-mentioned techniques developed using melittin were adapted for CypA. Comparisons of d-uptake in the presence and absence of CsA shows the ligand to have a stabilising affect on the protein.
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Books on the topic "Conformation"

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Symposium on Protein Conformation (1991 : Ciba Foundation), ed. Protein conformation. Chichester [England]: Wiley, 1991.

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T, Peters, and Evans S. V. 1959-, eds. Bioactive conformation. Berlin: Springer, 2007.

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Bodega, Beatrice, and Chiara Lanzuolo, eds. Capturing Chromosome Conformation. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-0664-3.

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Peters, Thomas, ed. Bioactive Conformation I. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-49078-4.

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Peters, Thomas, ed. Bioactive Conformation II. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-49080-7.

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Raghavendra, Rao V. S., ed. Conformation of carbohydrates. Amsterdam, The Netherlands: Harwood Academic Publishers, 1998.

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Raghavendra, Rao V. S., ed. Conformation of carbohydrates. Australia: Harwood Academic Publishers, 1998.

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Schweda, Elke. Structural studies of some bacterial lipopolysaccharides and NMR and conformational studies of some mono- and disaccharide derivatives. Stockholm: Dept. of Organic Chemistry, Arrhenius Laboratory, University of Stockholm, 1987.

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Ohyama, Takashi. DNA Conformation and Transcription. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-29148-2.

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B, Roswell Linda, ed. Protein conformation: New research. New York: Nova Science Publishers, 2008.

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Book chapters on the topic "Conformation"

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Gooch, Jan W. "Conformation." In Encyclopedic Dictionary of Polymers, 166. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_2826.

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Elias, Hans-Georg. "Conformation." In Macromolecules, 137–51. D-69451 Weinheim, Germany: Wiley-VCH Verlag GmbH, 2014. http://dx.doi.org/10.1002/9783527627219.ch5.

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Tadros, Tharwat. "Polymer Conformation." In Encyclopedia of Colloid and Interface Science, 962–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-20665-8_132.

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Tarchevsky, I. A., and G. N. Marchenko. "Cellulose Conformation." In Heidelberger Lehrtexte Wirtschaftswissenschaften, 156–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75474-6_15.

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Schmiermund, Torsten. "Conformation Isomers." In essentials, 41–46. Wiesbaden: Springer Fachmedien Wiesbaden, 2021. http://dx.doi.org/10.1007/978-3-658-32035-5_8.

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Fowler, Murray E., and P. Walter Bravo. "Conformation and Gaits." In Medicine and Surgery of Camelids, 587–602. Ames, Iowa USA: Blackwell Publishing, Inc., 2013. http://dx.doi.org/10.1002/9781118785706.ch24.

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Fraser, James, Mathieu Rousseau, Mathieu Blanchette, and Josée Dostie. "Computing Chromosome Conformation." In Methods in Molecular Biology, 251–68. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-854-6_16.

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Maruyama, Osamu, Takayoshi Shoudai, Emiko Furuichi, Satoru Kuhara, and Satoru Miyano. "Learning Conformation Rules." In Discovery Science, 243–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/3-540-45650-3_22.

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Dascanio, John J. "Perineal Conformation Evaluation." In Equine Reproductive Procedures, 17–19. Hoboken, NJ, USA: John Wiley & Sons, Inc, 2014. http://dx.doi.org/10.1002/9781118904398.ch5.

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Pucéat, Michel. "Capturing Chromosome Conformation." In Methods in Molecular Biology, 1–7. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0664-3_1.

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Conference papers on the topic "Conformation"

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Golodnizky, Daniel, Carlos E. S. Bernardes, Maya Davidovich-Pinhas, Ronit Bitton, and Yulia Shmidov. "Isotropic liquid state of triacylglycerols: The starting point of fats and oils crystallization." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/ggfh1118.

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Over the years, several models of triacylglycerol (TAG) molecular conformations and bulk arrangements in isotropic liquid state have been proposed and are still up for debate. This organization is the starting state, from which the molecules self-assemble and form the initial stable nucleus, which then grows to form the solid crystal. The current research aims to explore the isotropic liquid state, while focusing on its impact on nucleation and crystal formation. This aim was addressed by implementing experimental methods, such as X-ray diffraction and small-angle X-ray scattering coupled with a computational method, such as molecular dynamics simulation. These techniques were used to study tristearin and triolein as models for saturated and unsaturated TAGs, respectively. Four different conformations were suggested for the two TAGs, and the results showed conformation abundancy in the order: trident (Tr) > chair (Ch) > propeller (Pr) > tuning-fork (Tf). The existence of clusters was demonstrated, each of which exhibited a heterogeneous distribution of conformations. The preferability to find a specific pair of conformations next to each other was analyzed and, surprisingly, it was found that Tf will preferably pair only with Tr although Tf is the preferable conformation in most crystal polymorphs. High general conversion rates from any conformation to another, and high specific conversion rates from and to the Tf conformation were calculated. It is proposed that the high conversion rates observed enable the crystallization process, despite the low proportion of Tf molecules. Overall, the results confirm the formation of specific structures in the liquid state, which combine all previously suggested models and further expand the knowledge using experimental and computational tools.
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Gavrilenkova, A. A., I. E. Deev, E. V. Bocharov, I. S. Okhrimenko, and O. V. Serova. "STUDY OF MECHANISMS OF ACTIVATION OF THE INSULIN-LIKE GROWTH FACTOR RECEPTOR (IGF-IR) USING MUTANT FORMS OF THE RECEPTOR." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-306.

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At the moment, a lot of research is being conducted to study the mechanisms of activation of the insulin receptor family, but the exact mechanisms of conformational changes in receptors during activation are still being investigated. It is assumed that in the inactive state, the TM domains of the insulin receptor are in a conformation that prevents the interaction of kinase domains. Binding to the ligand changes the conformation of the receptor, as a result, intracellular tyrosine kinase domains converge and cause a cellular response.
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Parise, L. V., B. Steiner, L. Nannizzi, and D. A. Phillips. "PEPTIDES FROM FIBRINOGENAND FIBRONECTIN CHANGE THE CONFORMATIONOF PURIFIED PLATELET GLYCOPROTEIN IIb-IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643697.

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Specific amino acid sequences in fibrinogen and fibronectin appear to mediate the binding of these ligands to the glycoprotein (GP) IIb-IIIacomplex in platelets. Thesesequences include LGGAKQAGDV from the y chain of fibrinogen, and RGD(S) from the a chain of fibrinogenand the cell-binding domain of fibronectin. Several recent reports suggest thatfibrinogen and/or peptides with these sequences cause clustering of GPIIb-IIIa on the platelet surface and Na+/H+ exchange in epinephrine-stimulated platelets. Thus, it is possible that occupancy of specific sites on GP Ilb-IIIa affects its conformation, initiating such events. In this study,we determined whether LGGAKQAGDV, RGDS, and related peptides affect the conformation of purified platelet GP IIb-IIIa. Conformational changes in GP IIb-IIIa were evaluated bychanges in proteolytic susceptibility and hydrodynamic properties. Thepurified GP IIb-IIIa complex was fund to be resistant to proteolysis bythrombin. However, pretreatment of GP IIb-IIIa with various peptidesincreased the susceptibility ofGP libα to thrombin-induced proteolysis,as quantitated onpolyacryfamide gels.The order of potency of these peptides was RGDS<LGGAKQAGDV < KGDS < RGES. This order of potency agrees with that for the abilityof these peptides to inhibit 125I-fibrinogen binding to platelets. The effect of the peptides on proteolysis was time-, temperature-, and concentration-dependent; RGDS Induced a half-maximal effect at ˜60μM. Evaluation of the hydrodynamic properties of GP IIb-IIIa showed that LGGAKQAGDV orRGDS, but not RGES, decreased thesedimentation coefficient of GP IIb-IIIa from 8.5S to 7.7 S or7.4, S,respectively. This changewas accompanied by an increase in theStoke’s radius from 73 A to 84 A. These results suggestthat LGGAKQAGDV andRGDS alterthe conformationof the purified GPIIb-IIIa heterodimer complex by causing it to unfold.This change in conformation may be related to changesin the distribution and function of GP IIb-IIIaon the platelet surface that occurwith occupancy ofligand binding sites.
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Cierniewski, C. S., and A. Z. Budzynski. "CONFORMATIONAL EQUILIBRIA IN THE γ CHAIN COOH-TERMINUS OF HUMAN FIBRINOGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642935.

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Synthetic peptides and fragments cleaved from native fibrinogen are used in studies to localize binding sites for various ligands. We addressed the question how the native conformation of a selected γ chain segment is affected by scission of the original chain. The conformation of the γ chain COOH-terminus of intact fibrinogen and its various fragments containing this region has been compared by an immunochemical analysis. An antibody population specific for the native epitope within the γ391-405 segment was isolated by affinity chromatography on the corresponding synthetic peptide. Between 19.2 and 22.8% of antibodies were obtained from three different antisera indicating that this region represents one of the major epitopes of native fibrinogen. Anti-γ391-405 antibodies were used to determine the value of Kconf the equilibrium constant for the interconversion of the non-native and native conformations of this epitope. The measurements were done using native fibrinogen, fragments D1 and DD, γ chain and γ391-405 synthetic peptide. In addition, the effect of 5 M guanidine-HCl on the conformation of fragments D1 and DD, which is known to abolish their antipolymerizing activity, was studied. Radioiodinated fibrinogen was used in the determination of Kconf, and quantitative analytical parameters, CI50% and CIs, calculated from competition between 125I-fibrinogen and the fibrinogen derivatives under study for binding to the immunochemically purified antibody. The measurements indicated that the epitope is unperturbed by iodination of fibrinogen and that 38.3% of fragment D1, 8.9% of fragment DD, 3.6% of the γ chain and less than 0.008% of the γ391-405 molecules adopt in aqueous solution the native conformation within the epitope. Denaturation of fragment D1 with 5 M guanidine-HCl affected only slightly the conformation of this γ chain determinant. More significant changes in the conformation were observed when fragment DD was denatured. The results suggest that long-range interactions are necessary for the stabilization of the native structure in the region of fibrinogen that interacts with the antibody and which is in close vicinity to the polymerization site, crosslinking site, and platelet recognition site.
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Bielça, Luciene Aparecida, Fernando Pacanelli Martins, and Messias Meneguette Júnior. "REPRESENTAÇÃO POR LOG-CONFORMATION." In Conferência Brasileira de Dinâmica, Controle e Aplicações. SBMAC, 2011. http://dx.doi.org/10.5540/dincon.2011.001.1.0123.

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Carreira, Beatriz Liara, Analice Costacurta Brandi, Laison Junio da Silva Furlan, Matheus Tozo de Araujo, and Leandro Franco de Souza. "Log-Conformation and Square Root-Conformation Transformations in High Weissenberg Number Flows." In 25th International Congress of Mechanical Engineering. ABCM, 2019. http://dx.doi.org/10.26678/abcm.cobem2019.cob2019-1949.

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Pratt, David W. "Methyl rotors in large molecules: probes of intramolecular vibrational relaxation and electronic structure." In OSA Annual Meeting. Washington, D.C.: Optica Publishing Group, 1990. http://dx.doi.org/10.1364/oam.1990.fg2.

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A methyl (CH3) group that is attached to a large molecule by a covalent bond adopts a preferred conformation with respect to nearby bonds and exhibits large-amplitude torsional motion. Both the preferred conformations and torsional motions are influenced by the local electronic environment. Additionally, the low-frequency torsional modes may couple to other molecular vibrational modes, providing a mechanism for intramolecular vibrational energy redistribution (IVR).
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Pohl, Radek, Dominik Rejman, Petr Kočalka, and Ivan Rosenberg. "Pyrrolidine nucleotide analogues – conformation study." In XIIIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2005. http://dx.doi.org/10.1135/css200507165.

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Ming Xu. "Distribution of macromolecule chain's conformation." In 2011 International Conference on Electronics and Optoelectronics (ICEOE). IEEE, 2011. http://dx.doi.org/10.1109/iceoe.2011.6013072.

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Serhal, D., M. Hajj, E. Rodes, and B. Jecko. "EBG antenna conformation for beamforming." In Propagation Conference (LAPC). IEEE, 2008. http://dx.doi.org/10.1109/lapc.2008.4516881.

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Reports on the topic "Conformation"

1

Kroll, D. M., and G. Gompper. The Conformation of Fluid Membranes: Monte Carlo Simulations. Fort Belvoir, VA: Defense Technical Information Center, February 1992. http://dx.doi.org/10.21236/ada271695.

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Zhu, Xiaoyang. Controlling Protein Conformation and Activities on Block-Copolymer Nanopatterns. Fort Belvoir, VA: Defense Technical Information Center, October 2013. http://dx.doi.org/10.21236/ada607976.

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Zhu, Xiaoyang, and Tim P. Lodge. Controlling Protein Conformation & Activities on Block-Copolymer Nanopatterns. Fort Belvoir, VA: Defense Technical Information Center, November 2009. http://dx.doi.org/10.21236/ada520626.

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Hunt, Nathaniel George. Theoretical study of the conformation and energy of supercoiled DNA. Office of Scientific and Technical Information (OSTI), January 1992. http://dx.doi.org/10.2172/10150925.

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Feng, J., A. G. MacDiarmid, and A. J. Epstein. Conformation of Polyaniline: Effect of Mechanical Shaking and Spin Casting. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada330203.

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Stock, Joseph D., Julia A. Calderón Díaz, Benny E. Mote, and Kenneth J. Stalder. Joint Angles for Feet and Leg Conformation Traits in Second Gestation Sows. Ames (Iowa): Iowa State University, January 2016. http://dx.doi.org/10.31274/ans_air-180814-249.

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Onteru, Suneel K., Bin Fan, Benny E. Mote, Timo Serenius, Marja Nikkilä, Kenneth J. Stalder, and Max F. Rothschild. Determination of Genes Associated with Leg and Body Conformation Traits in Pigs. Ames (Iowa): Iowa State University, January 2008. http://dx.doi.org/10.31274/ans_air-180814-987.

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Meza, J. C., and M. L. Martinez. A numerical study of hybrid optimization methods for the molecular conformation problems. Office of Scientific and Technical Information (OSTI), May 1993. http://dx.doi.org/10.2172/10175387.

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Caplan, Daniel Franz. NMR studies of the conformation and motion of tetrahydrofuran in graphite intercalation compounds. Office of Scientific and Technical Information (OSTI), November 1991. http://dx.doi.org/10.2172/10107524.

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Schaufele, Fred. Temporal and Spatial Dynamics of Androgen Receptor Conformation and Interactions in Prostate Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, November 2007. http://dx.doi.org/10.21236/ada477345.

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