دورية أكاديمية

Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes

التفاصيل البيبلوغرافية
العنوان: Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
المؤلفون: Johannes Schiebel, Roberto Gaspari, Tobias Wulsdorf, Khang Ngo, Christian Sohn, Tobias E. Schrader, Andrea Cavalli, Andreas Ostermann, Andreas Heine, Gerhard Klebe
المصدر: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
بيانات النشر: Nature Portfolio, 2018.
سنة النشر: 2018
المجموعة: LCC:Science
مصطلحات موضوعية: Science
الوصف: Trypsin is a serine protease. Here the authors present the high resolution X-ray and neutron diffraction structures of uncomplexed and inhibitor bound trypsin that provide insights into the geometry of H-bonds in the active site of the enzyme and molecular dynamics simulations reveal the kinetics of ligand binding induced desolvation.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2041-1723
Relation: https://doaj.org/toc/2041-1723
DOI: 10.1038/s41467-018-05769-2
URL الوصول: https://doaj.org/article/dfa101099f7848ffada5601ea4aa65b1
رقم الأكسشن: edsdoj.fa101099f7848ffada5601ea4aa65b1
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20411723
DOI:10.1038/s41467-018-05769-2