NMRSTRUCTPROT · NMR studies of protein structures
6РП — Действия „Мария Кюри“
- Период
- 2006-07-01 → 2009-06-30
- Финансиране от ЕС
- 272 721 €
- Участници
- 2
- Схема
- OIF
Линиите свързват координатора с партньорите. За проекти отпреди 2014 г. CORDIS не винаги дава точни координати. Тези точки са на ниво град или държава.
Накратко на български
Структурите и динамиката на протеините се анализират чрез ядрено магнитен резонанс, като например се проучва как една промяна в аминокиселината на липаза А влияе на термостабилността ѝ. Това помага за създаването на по-стабилни катализатори за нуждите на биотехнологиите и индустрията.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Резултати накратко
Final Activity Report Summary - NMRSTRUCTPROT (NMR studies of protein structures)
Nuclear magnetic resonance (NMR) is a tool used to determine the three-dimensional structure of a protein. NMR provides additional information about protein dynamics. This data can then be related to protein activity, such as interactions with drugs or catalytic properties. The outgoing phase project was part of the structural proteomics initiative, which aimed to determine all unknown protein folds, thus providing a large testing set for structure prediction tool development. Structures of two proteomics targets were determined using nuclear magnetic resonance (NMR) and two other structure determinations were also attempted. A protein selection procedure suitable for structure determination was developed. Modern equipment, namely a 1 mm diameter probe combined with robotics, allowed for high-throughput screening of proteins using low amounts of material. In addition, NMR screening was established as a tool to select folded proteins amenable for structure determination using X-ray crystallography. The return phase project aimed to determine factors responsible for protein thermostability. The thermal stability of proteins is of great importance in biotechnology and industry, where it is desired to use stable and robust catalysts. Lipase A from bacillus subtilis was used as a model protein for this study. Comparison of the structure and properties between two variants of the protein was performed. The mutants differed at only one amino-acid position which induced change in thermostability of 30 degrees Celsius. The studies were performed using NMR spectroscopy and X-ray crystallography and were in progress at the reporting date.
Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз
Цел на проекта
The outgoing phase: Structural proteomics is a large-scale project to determine a sufficiently large number of structures to be representative of all protein folds. This objective is approached using high-throughput protein preparation and structure determination with X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. My particular interest involves the use of NMR spectroscopy in structural proteomics.The development of NMR spectroscopy for structural proteomics of Thermotoga maritima is a major focus of the research group of Professor Kurt Wüthrich at The Scripps Research Institute, which forms a part of the Joint Centre for Structural Genomics.About 60% of T. maritima proteins do not have predicted structural annotations, and their levels of homology to proteins with known structures are lower than 30%. The structurally unpredictable proteins with fewer than 150 amino acid residues will be targets for my structural studies. The structures of proteins exhibiting promising NMR spectra will be determined using NMR spectroscopy. The determined structures will provide a basis for further functional studies. The return phase: Enzymes are of great interest to chemical and pharmaceutical industry as asymmetric catalysts. Humicola lanuginosa lipase (HLL) hydrolyses water-insoluble esters, and is applied as a detergent constituent. The proposed research deals with the studies on structural basis of HLL enantioselectivity.The enzyme will be in vitro evolved towards improved enantioselectivity by a number of cycles involving:i) introduction of mutations, andii) selection of improved HLL using high-throughput screening method.The structure of the evolved protein will be studied with NMR spectroscopy. Comparison of the obtained structure with the wild type will reveal structural basis of HLL enantioselectivity.
Оригинален текст от CORDIS (на английски).
Участници
- MAX-PLANCK-INSTITUT FUR KOHLENFORSCHUNG · MULHEIM AN DER RUHRКоординаторНиво градГермания
- THE SCRIPPS RESEARCH INSTITUTE · LA JOLLAСъединени щати
Връзки
Данни: CORDIS, © Европейски съюз