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Determination Par Rmn De Structures 3d De Peptides Et De Proteines
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Book Synopsis Détermination Par Rmn de Structures 3d de Peptides Et de Protéines by : Emeric Wasielewski
Download or read book Détermination Par Rmn de Structures 3d de Peptides Et de Protéines written by Emeric Wasielewski and published by Omniscriptum. This book was released on 2011-05 with total page 200 pages. Available in PDF, EPUB and Kindle. Book excerpt: Les fonctions sp cifiques des prot ines r sultent de leurs caract ristiques structurales et dynamiques. La spectroscopie RMN apporte ces deux informations, avec des strat gies d' tudes diff rentes selon la taille des biomol cules. Ce travail pr sente les tudes par RMN de deux types de mol cules intervenant dans deux contextes biologiques diff rents. D'abord le m tabolisme du fer chez les bact ries Gram-n gatif: compr hension de la reconnaissance sp cifique complexe m tallique sid rophore/r cepteur membranaire. Deux sid rophores peptidiques bact riens ont t tudi s (azoverdine d'Azomonas macrocytogenes ATCC 12334 et pyoverdine PaA de Pseudomonas aeruginosa ATCC 15692) en adaptant des m thodes utilis es sur les prot ines (HNCA en abondance naturelle de 13C, couplages dipolaires r siduels (RDC)). Le cas de conform res de PaA en change chimique interm diaire a t tudi . Ensuite la transcription et la r paration de l'ADN via l' tude de trois domaines de sous-unit s du facteur humain de transcription/r paration TFIIH: MAT1 (domaine RING C3HC4), p44 (dynamique et propri t s d' change m tallique du domaine RING C8) et p62 (utilisation des RDC pour le domaine PH).
Book Synopsis DETERMINATION, PAR RMN, DE LA STRUCTURE TRIDIMENSIONNELLE DES PEPTIDES ET DES PROTEINES by : YINSHAN.. YANG
Download or read book DETERMINATION, PAR RMN, DE LA STRUCTURE TRIDIMENSIONNELLE DES PEPTIDES ET DES PROTEINES written by YINSHAN.. YANG and published by . This book was released on 1993 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: CE TRAVAIL A PERMIS, GRACE A DES TECHNIQUES DE RESONANCE MAGNETIQUE NUCLEAIRE (RMN) A 2 ET 3 DIMENSIONS, A L'ETUDE CONFORMATIONNELLE DE PEPTIDES ET DE PROTEINES EN SOLUTION. UNE PREMIERE APPLICATION CONCERNE UN PEPTIDE (23 ACIDES AMINES) ISSU DE LA BRANCHE N-TERMINALE DE L'ASPARTYL-TARN SYNTHETASE. IL A ETE MONTRE PAR DES EXPERIENCES DE DICHROISME CIRCULAIRE QUE LE PEPTIDE EN SOLUTION AQUEUSE INTERAGIT AVEC POLY(DT). LA TECHNIQUE DE RMN 2D A ETE UTILISEE POUR ATTRIBUER LES SPECTRES PROTON. SUR LA BASE DES CONTRAINTES DE DISTANCES INTER-PROTONIQUE TIREES DES EXPERIENCES NOESY, LA STRUCTURE TRIDIMENSIONNELLE DU PEPTIDE A ETE DETERMINEE. ENSUITE LA TRANSITION CONFORMATIONNELLE D'UNE PROTEINE, L'ALPHA-COBRATOXINE (71 ACIDES AMINES) EN FONCTION DU PH A ETE ETUDIE. L'ATTRIBUTION COMPLETE DES RESONANCES PROTONIQUES A ETE REALISEE A PH NEUTRE PAR DIFFERENTES EXPERIENCES DE RMN 2D. LA RMN COUPLEE AUX CALCULS DE DYNAMIQUE MOLECULAIRE A MONTRE QUE LA CONFORMATION GLOBALE ETAIT CONSERVEE AVEC DES DIFFERENCES LOCALES EN PARTICULIER AU NIVEAU DE L'HISTIDINE 18. LA STRUCTURE D'UNE AUTRE PROTEINE, LA SOUS-UNITE A DE LA CROTOXINE (90 ACIDES AMINES) A ETE EGALEMENT ETUDIEE. L'ATTRIBUTION COMPLETE DES RESONANCES DU PROTON A L'AIDE DES EXPERIENCES RMN-2D ET 3D A ETE EFFECTUEE. LES CARTES 2D NOESY ONT PERMIS L'EVALUATION DES DISTANCES INTER-PROTONIQUES QUI CONSTITUENT AINSI LES CONTRAINTES POUR LES CALCULS DE DYNAMIQUE MOLECULAIRE
Book Synopsis On the Determination of Three-dimensional Protein Structures by Nuclear Magnetic Resonance Methods by : Per J. Kraulis
Download or read book On the Determination of Three-dimensional Protein Structures by Nuclear Magnetic Resonance Methods written by Per J. Kraulis and published by . This book was released on 1989 with total page 47 pages. Available in PDF, EPUB and Kindle. Book excerpt: During the last 10 years, nuclear magnetic resonance (NMR) methods have been developed to determine the three-dimensional structures of small proteins. This thesis reviews these methods and discusses their limitations. The assignment of the NMR spectrum of a protein is a necessary, bbut not sufficient, requirement for the determinetion of its structure by NMR methods.For this purpose, an interactive graphics program ANSIG has been developed. Spectrum contours can be viewed, and cross peaks extracted, connested and assigned. Assignment lists and distance restraints lists derived from NOESY cross peak intensities can be produced. A novel algorithm for the calculation of three-dimensional protein structures from inter-proton distance restraints derived ,from NMR data has been implemented in the program NOEDIA. A data base of crystallographically determined protein structured is searched for fragments that fit the data and the protein structure is built from them. Cecropin A, an antibacterial peptide from the giant silk moth HYALOPHORA CECROPIA, was investigated in a solution containing 15% hexafluoroisopropyl alchohol. The three-dimensional structure of the 37-residue peptide was computed from the NMR data ba the simulated dynamical annealing method. It consists of two amphiphatic a-helical regions 5-21 and 24-37, whose relative orientation could not be defined. The cellulases of the filamentous fungus TRICHODERMA REESEI contain a strongly conserved small terminal domain, which is the N-terminal in two of them and C-terminal in the other two. The structure of a synthetic 36-residue peptide corresponding to the C-terminal domain of cellobiohydrolase I was determined grom NMR data using a hybrid distance geometry-dynamic simulated annealing method. The molecule is wedge-shaped and consists of an irregular triplestranded anti-parallel B-sheet. The structure is very well defined due to extensive stereospecific assignments and permits analysis of a number of side chain interactions. The first example of a 3D NMR spectrum of a protein is presented. The combination of two 2D experiments into a 3D experiment facilitates cross peak assignment and potentially increases the size of proteins amenable to structure determination ba NMR.
Book Synopsis Structure des Proteines par RMN by :
Download or read book Structure des Proteines par RMN written by and published by Ed. Techniques Ingénieur. This book was released on with total page 18 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis RMN 20 ET 3D DES PEPTIDES ET DES PROTEINES. DEVELOPPEMENTS METHODOLOGIQUES ET APPLICATION A L'ETUDE D'UNE PROTEINE TRANSPORTEUSE DE PHOSPHOLIPIDES by : JEAN-PIERRE.. SIMORRE
Download or read book RMN 20 ET 3D DES PEPTIDES ET DES PROTEINES. DEVELOPPEMENTS METHODOLOGIQUES ET APPLICATION A L'ETUDE D'UNE PROTEINE TRANSPORTEUSE DE PHOSPHOLIPIDES written by JEAN-PIERRE.. SIMORRE and published by . This book was released on 1991 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: L'UTILISATION DES TECHNIQUES DE RMN 2D ET 3D A PERMIS L'ATTRIBUTION COMPLETE D'UNE PROTEINE CONSTITUEE DE 90 ACIDES AMINES ET LES PARAMETRES STRUCTURAUX NECESSAIRES POUR DETERMINER SA CONFORMATION TRIDIMENSIONNELLE ONT ETE EXTRAITS. LES TECHNIQUES DE RMN 3D HOMONUCLEAIRE MISES EN PLACE DURANT CETTE THESE ONT FAIT L'OBJET D'AMELIORATIONS TENDANT A ELIMINER CORRECTEMENT LE SIGNAL DE L'EAU, A SUPPRIMER LES ARTEFACTS, A OPTIMISER LES TRANSFERTS HOHAHA AINSI QU'A AUGMENTER LA RESOLUTION SANS ACCROITRE LES TEMPS D'EXPERIENCE. UNE AUTRE PARTIR DU TRAVAIL A PORTE SUR LA MISE EN EVIDENCE DES MOUVEMENTS INTRAMOLECULAIRES D'UN PEPTIDE. IL S'AGISSAIT D'INTERPRETER PLUS CORRECTEMENT LES EFFETS NOE EN TERMES DE CONTRAINTES DE DISTANCE
Book Synopsis ETUDE STRUCTURALE PAR RMN DE PEPTIDES ET PROTEINES DU SYSTEME VASOREGULATEUR by : PHILIPPE.. SIZUN
Download or read book ETUDE STRUCTURALE PAR RMN DE PEPTIDES ET PROTEINES DU SYSTEME VASOREGULATEUR written by PHILIPPE.. SIZUN and published by . This book was released on 1991 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: L'OBJECTIF PRINCIPAL DE CE TRAVAIL EST DE MONTRER COMMENT LA RESONANCE MAGNETIQUE NUCLEAIRE (RMN) PERMET D'ACCEDER A LA STRUCTURE TRIDIMENSIONNELLE DE PEPTIDES ET DE PROTEINES EN SOLUTION. L'ETUDE COMPAREE DE COMPOSES VASOREGULATEURS ALLANT DE PETITS PEPTIDES HORMONAUX A UNE PROTEINE DE 65 RESIDUS, L'HIRUDINE A PERMIS DE DEGAGER LES STRATEGIES 1D ET 2D LES PLUS APPROPRIEES. IL EST APPARU QUE LA TAILLE DU PEPTIDE JOUE UN ROLE FONDAMENTAL DANS LA PROBABILITE DE STRUCTURATION EN SOLUTION, L'ABSENCE DE COOPERATIVITE LIMITANT AINSI LA MOBILITE STRUCTURALE DE PETITS PEPTIDES. CETTE DERNIERE CROIT DES QUE LA TAILLE AUGMENTE OU QUE DES POINTS DE BLOCAGE CONFORMATIONNELS (PONTS DISULFURE) EXISTENT. POUR UNE PROTEINE TELLE QUE L'HIRUDINE, LA COMBINAISON DES DONNEES RMN EXTRAITE D'EXPERIENCES SPECIFIQUES (DEPLACEMENTS CHIMIQUES CONSTANTES DE COUPLAGE, EFFETS OVERHAUSER, ACCESSIBILITE DES PROTONS AMIDES) ET DE LA MODELISATION MOLECULAIRE CONTRAINTE A PERMIS DE PROPOSER UNE STRUCTURE 3D EN SOLUTION. UNE ANALYSE COMPARATIVE DES STRUCTURES OBTENUES ET DE CELLES PREVISIBLES GRACE AUX METHODES DE PREDICTION A MIS EN LUMIERE LA NOTION DE PREDISPOSITION CONFORMATIONNELLE POUVANT SERVIR DE BASE AUX ETUDES DE RELATION STRUCTURE-ACTIVITE
Book Synopsis DETERMINATION PAR RMN DE LA STRUCTURE DE PROTEINES EN SOLUTION by : AFAF.. MIKOU
Download or read book DETERMINATION PAR RMN DE LA STRUCTURE DE PROTEINES EN SOLUTION written by AFAF.. MIKOU and published by . This book was released on 1990 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: DANS LE CADRE DE L'ETUDE DE LA RELATION STRUCTURE-ACTIVITE, CE TRAVAIL SE PROPOSE D'ETABLIR UNE STRATEGIE DE DETERMINATION, PAR RESONANCE MAGNETIQUE NUCLEAIRE (RMN), DE STRUCTURE DE PROTEINES EN SOLUTION. POUR CE FAIRE, TOUTES LES ETAPES DE L'ETUDE CONFORMATIONNELLE D'UNE PROTEINE SONT DECRITES DEPUIS L'ECHANTILLON DANS UN TUBE RMN JUSQU'A LA STRUCTURE TERTIAIRE EN SOLUTION. DANS CETTE DEMARCHE GENERALE, L'ATTRIBUTION DES RESONANCES AUX DIVERS PROTONS EST UNE ETAPE CLE. UNE STRATEGIE ORIGINALE D'ATTRIBUTION EST DECRITE: ELLE SE COMPOSE D'UNE VARIANTE DE LA METHODE DES SIGNATURES (MAIN CHAIN DIRECTED) QUI PERMET D'IDENTIFIER RAPIDEMENT LES STRUCTURES SECONDAIRES COMPLETEES PAR L'ATTRIBUTION SEQUENTIELLE CLASSIQUE. LA METHODE A ETE APPLIQUEE A L'ATTRIBUTION COMPLETE DE DEUX TOXINES: L'ALPHA COBRATOXINE (71 ACIDES AMINES) EXTRAITE DU VENIN DU NAJA NAJA SIAMENSIS ET LA TOXINE III (64 ACIDES AMINES) DU SCORPION ANDROCTONUS AUSTRALIS HECTOR. L'ANALYSE DETAILLEE ET PRECISE DES CARTES NOESY A CONDUIT A UN GRAND NOMBRE DE CONTRAINTES DE DISTANCES INTERPROTONIQUES. CES CONTRAINTES STRUCTURALES ONT ETE INCORPOREES DANS DES CALCULS DE CONVERSION DISTANCE-GEOMETRIE (VEMBED) ET DE DYNAMIQUE MOLECULAIRE (AMBER). POUR CHACUNE DES DEUX TOXINES, UNE STRUCTURE PRELIMINAIRE EST OBTENUE ET EST ACTUELLEMENT EN COURS DE RAFFINEMENT
Download or read book Biochemistry and Cell Biology written by and published by . This book was released on 1991 with total page 470 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Analysis of Nmr Chemical Shifts in Peptide and Protein Structure Determination by : Liya Wang
Download or read book Analysis of Nmr Chemical Shifts in Peptide and Protein Structure Determination written by Liya Wang and published by . This book was released on 2008 with total page 236 pages. Available in PDF, EPUB and Kindle. Book excerpt: Chemical shifts provide detailed information about non-covalent structure, solvent interactions, ionization constants, ring orientations, hydrogen bond interactions, and other phenomena. Since different chemical shift data sets are not necessarily comparable without corrections or adjustments, the applicability of statistical analysis of NMR chemical shifts to biomolecules has so far been limited. We use the term "congruent" to describe data sets that can be directly used for statistical analysis after proper adjustments. Congruence problems in chemical shift analysis can occur at three different levels. (1) At the protein level, when using collections of chemical shifts of proteins reported by different groups. (2) At the residue level, when using collections of chemical shifts of different residues, here random coil chemical shifts must be subtracted. (3) At the refined residue level, when using collections of chemical shifts of same residues, neighboring residue effects on the chemical shifts need to be taken into account. In this book, these correction or adjustment problems are addressed based on the newly proposed robust statistical models.
Book Synopsis Protein NMR Techniques by : A. Kristina Downing
Download or read book Protein NMR Techniques written by A. Kristina Downing and published by Springer Science & Business Media. This book was released on 2008-02-03 with total page 494 pages. Available in PDF, EPUB and Kindle. Book excerpt: When I was asked to edit the second edition of Protein NMR Techniques, my first thought was that the time was ripe for a new edition. The past several years have seen a surge in the development of novel methods that are truly revolutionizing our ability to characterize biological macromolecules in terms of speed, accuracy, and size limitations. I was particularly excited at the prospect of making these techniques accessible to all NMR labs and for the opportunity to ask the experts to divulge their hints and tips and to write, practically, about the methods. I commissioned 19 chapters with wide scope for Protein NMR Techniques, and the volume has been organized with numerous themes in mind. Chapters 1 and 2 deal with recombinant protein expression using two organisms, E. coli and P. pastoris, that can produce high yields of isotopically labeled protein at a reasonable cost. Staying with the idea of isotopic labeling, Chapter 3 describes methods for perdeuteration and site-specific protonation and is the first of several chapters in the book that is relevant to studies of higher molecular weight systems. A different, but equally powerful, method that uses molecular biology to “edit” the spectrum of a large molecule using segmental labeling is presented in Chapter 4. Having successfully produced a high molecular weight target for study, the next logical step is data acquisition. Hence, the final chapter on this theme, Chapter 5, describes TROSY methods for stru- ural studies.
Book Synopsis Détermination de la structure par RMN d'une protéine impliquée dans la biosynthèse de centres [Fe-S], SufA by : Nicolas Duraffourg
Download or read book Détermination de la structure par RMN d'une protéine impliquée dans la biosynthèse de centres [Fe-S], SufA written by Nicolas Duraffourg and published by . This book was released on 2007 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: La protéine SufA d'Escherichia coli est une protéine homodimérique, dite d'échafaudage, qui permet l'assemblage de centres [Fe-S] avant de les transmettre à une protéine cible possèdant une fonction biologique. Elle appartient à un ensemble de protéines organisées en opéron (SUF) qui semble activé dans le cadre de stress oxydatif. Afin de mieux comprendre le mode de fixation du centre [Fe-S] par la protéine SufA, la détermination de la structure tridimensionnelle par RMN a été entreprise. Nous avons obtenu la structure monomérique de la protéine sans son centre [Fe-S] (forme apo) et effectué des études de résonance magnétique nucléaire (RMN) préliminaires de la protéine SufA avec son centre métallique reconstitué. Nous avons pu ainsi observer trois résidus cystéine, que des études biochimiques ont montré comme étant impliqués dans la chélation du centre [Fe-S], et affirmer qu'ils étaient proches du site métallique sans toutefois définir exactement le mode de coordination du centre [Fe-S]. La détermination de la structure du dimère, en cours, et des études RMN complémentaires sur l'holoprotéine (avec son centre [Fe-S]) devrait nous permettre de répondre à ces questions toujours en suspens. D'autre part nous avons observé des différences structurales par rapport aux structures cristallographiques (publiées au cours de ce travail de thèse), particulièrement dans la partie C-terminale de la protéine où se situent deux des cystéines observées.
Book Synopsis DETERMINATION DE LA STRUCTURE TRIDIMENSIONNELLE DE PROTEINES EN SOLUTION PAR R.M.N. by : REMI.. LE GOAS
Download or read book DETERMINATION DE LA STRUCTURE TRIDIMENSIONNELLE DE PROTEINES EN SOLUTION PAR R.M.N. written by REMI.. LE GOAS and published by . This book was released on 1991 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: LA RESONANCE MAGNETIQUE NUCLEAIRE PERMET L'ETUDE DES PROTEINES EN SOLUTION, AUSSI BIEN D'UN POINT DE VUE STRUCTURAL QUE DYNAMIQUE. APRES UN RAPPEL DES PROPRIETES DETERMINANTES DE LA STRUCTURE TRIDIMENSIONNELLE DES PROTEINES, SONT ABORDEES LES EXPERIENCES MAJEURES DE LA R.M.N. A DEUX DIMENSIONS, QUI DELIVRENT LES PARAMETRES NECESSAIRES A LA RECONSTRUCTION D'UN MODELE STRUCTURAL (DISTANCES INTER-HYDROGENES ET ANGLES DIEDRES). L'OBTENTION DE CE MODELE REPOSE, D'UNE PART SUR L'ANALYSE CORRECTE DES DISTANCES ISSUES DES EXPERIENCES, D'AUTRE PART SUR L'UTILISATION D'ALGORITHMES INFORMATIQUES PERMETTANT DE PARCOURIR EFFICACEMENT L'ESPACE CONFORMATIONNEL, TELS QUE LA METHODE DE DISTANCE-GEOMETRIE ET LA DYNAMIQUE MOLECULAIRE. UNE STRATEGIE HYBRIDE UTILISANT SUCCESSIVEMENT LES DEUX TYPES D'ALGORITHME A ETE EMPLOYEE SUR L'ALPHA-COBRATOXINE (71 ACIDES AMINES): ELLE A PERMIS L'EVALUATION DES DEUX METHODES ET A CONDUIT A UN ENSEMBLE DE SOLUTIONS STRUCTURALES QUI SONT COMPAREES AVEC LE MODELE CRISTALLOGRAPHIQUE INDEPENDAMMENT PROPOSE
Book Synopsis Computational Development Towards High-throughput NMR-based Protein Structure Determination by :
Download or read book Computational Development Towards High-throughput NMR-based Protein Structure Determination written by and published by . This book was released on 2013 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Three-dimensional structures of proteins determined in solution by NMR spectroscopy have the unique advantage of revealing details of molecular structure and dynamics in a physiologically relevant state; however, the many tedious steps needed to solve and validate a structure make this method challenging. The barriers to NMR structure determination become higher for larger proteins whose spectra are harder to resolve. It is clear that advances need to be made in automating protein structure determination by NMR spectroscopy. The goal of my research has been to use computational methods to advance the development of high-throughput NMR spectroscopy. Accelerating and streamlining the structure determination process will enable investigators to spend less time solving structures and more time investigating challenging biomolecular systems. My goals have been to develop an automation protocol that integrates multiple steps, ensures the robustness of each step, incorporates iterative corrections, and includes visualization tools to validate and extend the results. I developed PINE-SPARKY as a graphical interface for checking and extending automated assignments made by the PINE-NMR server. ADAPT-NMR directs fast data collection by reduced dimensionality on the basis of ongoing NMR assignments. I helped develop a version of ADAPT-NMR (originally only for Varian spectrometers) for Bruker spectrometers, and I created ADAPT-NMR Enhancer as a visualization tool for validating and extending assignments made by ADAPT-NMR on either spectrometer system. I developed the PONDEROSA package to automate the next steps. PONDEROSA carries out automatic picking of 3D-NOESY peaks and iterative structure determinations with the protein sequence and the assignments as inputs. These automation and visualization tools cover almost all of the steps involved in protein structure determination by NMR spectroscopy. As a practical test of this technology, I solved the structure of the 2A proteinase from the human rhinovirus. As a side project, I built a relational database (PACSY DB) that combines information from the Protein Data Bank (PDB) and the Biological Magnetic Resonance data Bank (BMRB) and incorporates tools for structure analysis. PACSY DB can carry out complex queries that combine atomic coordinates, NMR parameters, and structural features of proteins.
Book Synopsis Determination of the Structure of Model Peptides Derived from Intracrystalline Biomineralization Protein, SM50, by PFG-enhanced NMR Experiments by : Guangzhao Xu
Download or read book Determination of the Structure of Model Peptides Derived from Intracrystalline Biomineralization Protein, SM50, by PFG-enhanced NMR Experiments written by Guangzhao Xu and published by . This book was released on 2000 with total page 424 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Protein Structure Determination by Paramagnetic NMR and Computational Hybrid Approach by : Kala Bharath Pilla
Download or read book Protein Structure Determination by Paramagnetic NMR and Computational Hybrid Approach written by Kala Bharath Pilla and published by . This book was released on 2015 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Computational modelling of proteins that rely on either de novo or evolutionary based approaches often produce poor quality structures, primarily due to the limitations in their algorithms or forcefields. Traditional experimental techniques such as X-ray crystallography depend on narrow set of crystallographic conditions while solution/solid state nuclear magnetic resonance (NMR) spectroscopy relies on cumbersome spectral analysis and complete resonance assignments. These traditional approaches are slow and costly endeavours. Computational/experimental hybrid approaches on the other hand provide a new avenue for reliable, rapid and cost-effective structure determination. Paramagnetic NMR offers easy generation of useful and sparse structural information which can be implemented as restraints in structure prediction algorithms. Pseudocontact shifts (PCS) are the most powerful of structural restraints generated by paramagnetic NMR which are long range in nature and can be easily obtained by simple 2D NMR experiments. This thesis demonstrates different approaches involved in protein structure calculations using PCS restraints in Rosetta. Chapter 2 demonstrates structure determination using PCS restraints exclusively obtained from protein samples in microcrystalline state by magic angle spinning (MAS) NMR spectroscopy. Chapter 3 discusses the implementation of using PCS data from multiple metal centres to precisely determine the location of spins in space in a manner analogues to GPS-satellites. Chapter 4 extends the usage of PCS data from multiple metal centres to capture distinct conformational states in proteins. Chapter 5 demonstrates new techniques especially developed for structure determination of large proteins involving super secondary structure motifs (Smotifs) and data driven iterative resampling. These different computational techniques serve the goal of determining accurate 3D models using minimal experimental data, which are applicable to proteins systems that are currently beyond the realm of traditional experimental approaches.
Book Synopsis A Probabilistic Approach to the Automation of NMR Protein Structure Determination by : Arash Bahrami
Download or read book A Probabilistic Approach to the Automation of NMR Protein Structure Determination written by Arash Bahrami and published by . This book was released on 2009 with total page 190 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Analyse de la structure tridimentionnelle des protéines par résonance magnétique nucléaire by : Anne Lesage
Download or read book Analyse de la structure tridimentionnelle des protéines par résonance magnétique nucléaire written by Anne Lesage and published by . This book was released on 1995 with total page 233 pages. Available in PDF, EPUB and Kindle. Book excerpt: Nous avons utilisé la résonance magnétique nucléaire d'une part pour l'étude structurale de peptides synthétiques mimant la jonction COL1-NC1 des collagènes FACIT, et d'autre part pour la détermination de la structure 3D du domaine d'interaction à l'ADN du régulateur transcriptionnel FRUR, domaine appelé FRUR (1-57). Les peptides ont été synthétisés et associés en trimères reliés par trois ponts disulfures inter-chaines. Les trimères formes ont été caractérisés par microsequençage, dichroîsme circulaire et RMN. Un modèle structural est proposé pour la jonction COL1-NC1 des collagènes FACIT. Des expériences RNM hétéronucleaires azote 15-proton à deux et trois dimensions ont été réalisées sur le domaine FRUR (1-57). Elles ont permis l'identification des effets nOe et la mesure des constantes de couplage HN-h : experiences 2D gHSQC, 3d NOESY-HMQC, 3D TOCSY-HMQC, 3D HNHA.
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