About: Nuclear magnetic resonance spectroscopy of proteins

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Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated.

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rdf:type	Thing yago:Ability105616246 yago:Abstraction100002137 yago:Cognition100023271 yago:Know-how105616786 yago:Method105660268 yago:PsychologicalFeature100023100 yago:WikicatProteinMethods
rdfs:label	مطيافية الرنين المغناطيسي النووي للبروتين (ar) Espectroscopia mediante resonancia magnética nuclear de proteínas (es) Spettroscopia a risonanza magnetica nucleare di proteine (it) Nuclear magnetic resonance spectroscopy of proteins (en) Ressonância magnética nuclear de proteínas (pt) ЯМР-спектроскопія білків (uk)
rdfs:comment	مطيافية الرنين المغناطيسي النووي للبروتين (بالإنجليزية: Nuclear magnetic resonance spectroscopy of proteins or protein NMR)‏ (مختصر عادة ان م ر لبروتين ) هي مجال من التي يستخدم فيها الرنين المغناطيسي الطيفي للحصول على معلومات حول بنية وديناميكية البروتينات. كانريتشارد إرنست وR. Wüthrich كورت رائدا في هذا ألمجال . و تقنيات مطيافية الرنين المغناطيسي النووي للبروتين تستخدم في كل من الأوساط الأكاديمية وصناعة التكنولوجيا الحيوية. تقرير التحليل الطيفي بواسطة NMR يتكون عادة من عدة مراحل ، استخدام كل مجموعة منفصلة من تقنيات عالية التخصص. ويتم إعداد العينة، يتم تعيين الأصداء، يتم إنشاء القيود ويحسب هيكل والتحقق من صحتها. (ar) La spettroscopia a risonanza magnetica nucleare di proteine (di solito abbreviata in NMR di proteine) è un campo della biologia strutturale nel quale la spettroscopia NMR è di solito usata per ottenere informazioni sulla struttura e le dinamiche delle proteine.Uno dei pionieri di questo campo di studio è stato, tra gli altri, Kurt Wüthrich, che ha ricevuto il Premio Nobel nel 2002. Le tecniche di NMR di proteine sono continuamente usate e migliorate sia nell'industria biotecnologica che in ambito accademico. (it) A espectroscopia mediante ressonância magnética nuclear de proteínas, também chamada de RMN de proteínas, é um campo da biologia estrutural no qual se utiliza espectroscopia RMN para obter informação sobre a estrutura e dinâmica das proteínas. O campo foi desenvolvido por Kurt Wüthrich entre outros, que compartilhou o Prémio Nobel de química em 2002. As técnicas de RMN utilizam-se de forma rotineira no âmbito académico e na indústria de biotecnologia. A determinação da estrutura das proteínas mediante espectroscopia RMN, no geral, consiste em várias fases sucessivas, cada uma delas utilizando um conjunto de técnicas altamente especializadas. A amostra é preparada, atribuem-se as ressonâncias, geram-se as restrições e calcula-se e valida-se a estrutura. (pt) ЯМР-спектроскопі́я білкі́в (Ядерна магнітно-резонансна спектроскопія білків; англ. Nuclear magnetic resonance spectroscopy of proteins) — метод структурної біології, в якому ЯМР-спектроскопія використовується для отримання інформації про структуру і динаміку білків (uk) La espectroscopia mediante resonancia magnética nuclear de proteínas (usualmente llamada RMN de proteínas) es un campo de la biología estructural en el cual se utiliza espectroscopia RMN para obtener información sobre la estructura y dinámica de las proteínas. El campo fue desarrollado por Kurt Wüthrich, entre otros, quién compartió el premio Nobel de química en 2002. Las técnicas de RMN se utilizan en forma rutinaria en el ámbito académico y en la industria de biotecnología. La determinación de la estructura de las proteínas mediante espectroscopia RMN por lo general consiste en varias fases sucesivas, cada una de ellas utilizando un conjunto de técnicas altamente especializadas. La muestra es preparada, se asignan las resonancias, se generan las restricciones y se calcula y valida la est (es) Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated. (en)
rdfs:seeAlso	Protein dynamics
foaf:depiction
dcterms:subject	Nuclear magnetic resonance spectroscopy Biophysics Protein structure Protein methods
Wikipage page ID	3654507 (xsd:integer)
Wikipage revision ID	1072266803 (xsd:integer)
Link from a Wikipage to another Wikipage	Caenorhabditis elegans Carbon-13 Nuclear magnetic resonance spectroscopy Proline Protein production Mole (unit) NMR Angstroms Deuterium Richard R. Ernst Variance J-coupling Protein crystallization Protein dynamics Nucleic acids NMR spectroscopy Radiofrequency Biophysics Chemical biology Gene expression Nuclear Overhauser effect Protein purification Pulse sequence GeNMR Genetic engineering Structural biology MRI Buffer solution WHAT IF software Correlation spectroscopy HNCA experiment HNCOCA experiment Karplus equation Ad Bax Amino acid Protein structure Crystallography and NMR system Drug development Nitrogen-15 Gerhard Wagner (physicist) Isotope Nitrogen-15 Isotopic labeling Protein Ramachandran plot Recombinant DNA Relaxation (NMR) Residual dipolar coupling Residue (chemistry) Harvard College Atomic nucleus Bacteriophage Magnetic fields Accuracy and precision Protein methods CheShift Chemical shift XPLOR-NIH Polyacrylamide gel Solid-state nuclear magnetic resonance HSPA1A Early pregnancy factor HSQC Kurt Wüthrich Nanometers National Institutes of Health Chaperone (protein) Sequential walking

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