Nuclear magnetic resonance spectroscopy of proteins (original) (raw)
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.
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| dbo:abstract | 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 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 estructura. (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. NMR involves the quantum-mechanical properties of the central core ("nucleus") of the atom. These properties depend on the local molecular environment, and their measurement provides a map of how the atoms are linked chemically, how close they are in space, and how rapidly they move with respect to each other. These properties are fundamentally the same as those used in the more familiar magnetic resonance imaging (MRI), but the molecular applications use a somewhat different approach, appropriate to the change of scale from millimeters (of interest to radiologists) to nanometers (bonded atoms are typically a fraction of a nanometer apart), a factor of a million. This change of scale requires much higher sensitivity of detection and stability for long term measurement. In contrast to MRI, structural biology studies do not directly generate an image, but rely on complex computer calculations to generate three-dimensional molecular models. Currently most samples are examined in a solution in water, but methods are being developed to also work with solid samples. Data collection relies on placing the sample inside a powerful magnet, sending radio frequency signals through the sample, and measuring the absorption of those signals. Depending on the environment of atoms within the protein, the nuclei of individual atoms will absorb different frequencies of radio signals. Furthermore, the absorption signals of different nuclei may be perturbed by adjacent nuclei. This information can be used to determine the distance between nuclei. These distances in turn can be used to determine the overall structure of the protein. A typical study might involve how two proteins interact with each other, possibly with a view to developing small molecules that can be used to probe the normal biology of the interaction ("chemical biology") or to provide possible leads for pharmaceutical use (drug development). Frequently, the interacting pair of proteins may have been identified by studies of human genetics, indicating the interaction can be disrupted by unfavorable mutations, or they may play a key role in the normal biology of a "model" organism like the fruit fly, yeast, the worm C. elegans, or mice. To prepare a sample, methods of molecular biology are typically used to make quantities by bacterial fermentation. This also permits changing the isotopic composition of the molecule, which is desirable because the isotopes behave differently and provide methods for identifying overlapping NMR signals. (en) 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) |
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| 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: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) |
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