Topic
Structural biology
About: Structural biology is a research topic. Over the lifetime, 2206 publications have been published within this topic receiving 126070 citations.
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TL;DR: The method to image and reveal structural details of proteins on a truly single-molecule level is reported, using low-energy electron holography to image individual proteins electrospray deposited on freestanding graphene.
Abstract: Imaging single proteins has been a long-standing ambition for advancing various fields in natural science, as for instance structural biology, biophysics, and molecular nanotechnology. In particular, revealing the distinct conformations of an individual protein is of utmost importance. Here, we show the imaging of individual proteins and protein complexes by low-energy electron holography. Samples of individual proteins and protein complexes on ultraclean freestanding graphene were prepared by soft-landing electrospray ion beam deposition, which allows chemical- and conformational-specific selection and gentle deposition. Low-energy electrons do not induce radiation damage, which enables acquiring subnanometer resolution images of individual proteins (cytochrome C and BSA) as well as of protein complexes (hemoglobin), which are not the result of an averaging process.
88 citations
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TL;DR: Understanding of the assembly, action, and regulation of the alternative pathway convertase has been significantly enhanced, and the structural determinants of some of these changes have been defined from structural and mutational analyses of the two enzymes.
Abstract: Complement convertases are bimolecular complexes expressing protease activity only against C3 and C5. Their action is necessary for production of the biological activities of the complement system. Formation of these complexes proceeds through sequential protein-protein interactions and proteolytic cleavages of high specificity. Recent structural, mutational and functional data on factors D and B have significantly enhanced our understanding of the assembly, action, and regulation of the alternative pathway convertase. These processes were shown to depend critically on conformational changes, only some of which are reversible. The need for such changes is dictated by the zymogen-like configurations of the active centers of these unique serine proteases. The structural determinants of some of these changes have been defined from structural and mutational analyses of the two enzymes. Transition of factor D from the zymogen-like to the catalytically active conformation is completely reversible, while the active conformation of the catalytic center of the Bb fragment of factor B is irreversibly attenuated to a great extent on dissociation of the convertase complex. Both mechanisms contribute to the regulation of the proteolytic activity of these enzymes. Additional studies are necessary for a complete description of the elegant mechanisms mediating these processes.
88 citations
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TL;DR: The recent progress made in the structural biology of both the relaxosome and the T4SS is described, which are mediated by type IV secretion systems.
88 citations
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TL;DR: A concise overview of recent developments in computational biophysics of membrane proteins is provided, using GPCRs as an example to showcase important information that can be derived from modern MD simulations.
88 citations
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TL;DR: The purpose of this review is to focus on the architecture of the C1 complex and the mechanisms underlying its activation and proteolytic activity, with particular emphasis on the modular proteases C1r and C1s.
88 citations