Synthetic mimetics of protein secondary structure domains
نویسندگان
چکیده
منابع مشابه
Synthetic mimetics of protein secondary structure domains
Proteins modulate the majority of all biological functions and are primarily composed of highly organized secondary structural elements such as helices, turns and sheets. Many of these functions are affected by a small number of key protein-protein contacts, often involving one or more of these well-defined structural elements. Given the ubiquitous nature of these protein recognition domains, t...
متن کاملChemogenomics with protein secondary-structure mimetics.
During molecular recognition of proteins in biological systems, helices, reverse turns, and beta-sheets are dominant motifs. Often there are therapeutic reasons for blocking such recognition sites, and significant progress has been made by medicinal chemists in the design and synthesis of semirigid molecular scaffolds on which to display amino acid side chains. The basic premise is that preorga...
متن کاملProtein Secondary Structure Mimetics as Modulators of Protein–Protein and Protein–Ligand Interactions•
The development of low-molecular-weight agents that modulate protein–protein interactions has been regarded as a difficult goal due to the relatively large and featureless protein interfacial surfaces involved [1–3]. Conventional methods for identifying inhibitors of protein–protein interactions generally involve the preparation and screening of large chemical libraries to discover lead compoun...
متن کاملHydrogen-bonded synthetic mimics of protein secondary structure as disruptors of protein-protein interactions.
Small molecules which can mimic the key structural facets of protein secondary structure, in particular the α-helix, β-strand, and β-sheet, have been shown to be potent disruptors of protein-protein interactions. Researchers have recently taken the organizational imitation of protein secondary structure to a new level by using intramolecular hydrogen bonds as stabilizing forces in these small m...
متن کاملImmunogenic Domains and Secondary Structure of Escherichia coli Recombinant Secreted Protein Escherichia coli-Secreted Protein B
Several pathogenic bacteria are able to induce the attaching and effacing (A/E) lesion. The A/E lesion is caused by effector proteins, such as Escherichia coli-secreted protein B (EspB), responsible together with Escherichia coli-secreted protein D for forming a pore structure on the host cell, which allows the translocation of effector proteins. Different variants of this protein can be found ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences
سال: 2010
ISSN: 1364-503X,1471-2962
DOI: 10.1098/rsta.2009.0210