3K1045 Analysis of molecular recognition mechanism using molecular recognition database
نویسندگان
چکیده
منابع مشابه
Analysis of molecular recognition using optical biosensors.
Optical biosensors have made the analysis of molecular interactions rapid and convenient. The field is still young, with commercial instrumentation having been available for less than ten years. For this reason instrument development is still an important factor and the past year has seen continuing advances in instrumentation and particularly in novel sensor surfaces.
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Molecular chaperones are essential in aiding client proteins to fold into their native structure and in maintaining cellular protein homeostasis. However, mechanistic aspects of chaperone function are still not well understood at the atomic level. We use nuclear magnetic resonance spectroscopy to elucidate the mechanism underlying client recognition by the adenosine triphosphate-independent cha...
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Several proteomic studies in the last decade revealed that many proteins are either completely disordered or possess long structurally flexible regions. Many such regions were shown to be of functional importance, often allowing a protein to interact with a large number of diverse partners. Parallel to these findings, during the last five years structural bioinformatics has produced an explosio...
متن کاملmpMoRFsDB: a database of molecular recognition features in membrane proteins
SUMMARY Molecular recognition features (MoRFs) are small, intrinsically disordered regions in proteins that undergo a disorder-to-order transition on binding to their partners. MoRFs are involved in protein-protein interactions and may function as the initial step in molecular recognition. The aim of this work was to collect, organize and store all membrane proteins that contain MoRFs. Membrane...
متن کاملMolecular mechanism of multispecific recognition of Calmodulin through conformational changes.
Calmodulin (CaM) is found to have the capability to bind multiple targets. Investigations on the association mechanism of CaM to its targets are crucial for understanding protein-protein binding and recognition. Here, we developed a structure-based model to explore the binding process between CaM and skMLCK binding peptide. We found the cooperation between nonnative electrostatic interaction an...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2002
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.42.s180_4