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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: In-cell NMR has become a unique technology for its ability to obtain the function-related structural information of the target proteins under the physiological or pathological cellular environments, which cannot be reconstituted in vitro.
22 citations
TL;DR: The crystal structure of Arabidopsis thaliana legumain isoform β (AtLEGβ) revealed unrestricted nonprime substrate binding pockets, consistent with the broad substrate specificity, as determined by degradomic assays, and it is shown that AtLEG β exhibits a true peptide ligase activity.
22 citations
TL;DR: This work proposes a general approach with a finite number of steps which allows one to localize the underlying problem of poor expression of a membrane protein using bR as an example and achieves increased bR expression by two orders of magnitude through the introduction of two silent mutations into bR coding DNA.
Abstract: Heterologous overexpression of functional membrane proteins is a major bottleneck of structural biology. Bacteriorhodopsin from Halobium salinarum (bR) is a striking example of the difficulties in membrane protein overexpression. We suggest a general approach with a finite number of steps which allows one to localize the underlying problem of poor expression of a membrane protein using bR as an example. Our approach is based on constructing chimeric proteins comprising parts of a protein of interest and complementary parts of a homologous protein demonstrating advantageous expression. This complementary protein approach allowed us to increase bR expression by two orders of magnitude through the introduction of two silent mutations into bR coding DNA. For the first time the high quality crystals of bR expressed in E. Coli were obtained using the produced protein. The crystals obtained with in meso nanovolume crystallization diffracted to 1.67 A.
22 citations
TL;DR: This chapter describes what is known thus far about the structures and functions of the handful of proteins encoded by filovirus genomes and describes for components of the nucleocapsid, the matrix, and the surface and secreted glycoproteins.
Abstract: In this chapter, we describe what is known thus far about the structures and functions of the handful of proteins encoded by filovirus genomes. Amongst the fascinating findings of the last decade is the plurality of functions and structures that these polypeptides can adopt. Many of the encoded proteins can play multiple, distinct roles in the virus life cycle, although the mechanisms by which these functions are determined and controlled remain mostly veiled. Further, some filovirus proteins are multistructural: adopting different oligomeric assemblies and sometimes, different tertiary structures to achieve their separate, and equally essential functions. Structures, and the functions they dictate, are described for components of the nucleocapsid, the matrix, and the surface and secreted glycoproteins.
22 citations
TL;DR: The available structural knowledge about proteins involved in trinucleotide expansion diseases and how this may influence the current means of investigation are discussed.
22 citations