Enabling time-resolved structural studies of biological macromolecules
نویسندگان
چکیده
منابع مشابه
Structural database resources for biological macromolecules
This Briefing reviews the widely used, currently active, up-to-date databases derived from the worldwide Protein Data Bank (PDB) to facilitate browsing, finding and exploring its entries. These databases contain visualization and analysis tools tailored to specific kinds of molecules and interactions, often including also complex metrics precomputed by experts or external programs, and connecti...
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Small-angle scattering (SAS) of x-rays and neutrons is a fundamental tool in the study of biological macromolecules. The major advantage of the method lies in its ability to provide structural information about partially or completely disordered systems. SAS allows one to study the structure of native particles in near physiological environments and to analyse structural changes in response to ...
متن کاملCrystallography of Biological Macromolecules
Src homology 2 domain-containing protein tyrosine phosphatase [SHP] substrate 1 (SHPS-1), a receptor-type transmembrane glycoprotein whose cytoplasmic region binds and activates the protein tyrosine phosphatases SHP-1 and SHP-2, and thereby modulates multiple cellular functions. Its extracellular region regulates intercellular communication in the neural and immune systems through its associati...
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C218 located at the interface between A-band and M-line. It has been shown by Centner et al. [2] that MURF-1, a member of the RING finger proteins, binds to the two Ig-domains A168 and A169 in proximity to the kinase. Thus, its binding might be involved in the regulation of titin kinase. The structure of this tandem Ig domain has been solved. Ig domains, also in titin, are involved in many prot...
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Carboxypeptidase Y (CPY) inhibitor I from the yeast, consisting of 204 amino acid residues, belongs to the phosphatidylethanolaminebinding protein (PEBP) family. The 2.7 Å crystal structure of the ICPY complex has been solved by molecular replacement [1, 2]. The structure of I consists of a major -type domain and an Nterminal helical segment. I has two CPY-binding sites: the N-terminal inhibito...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations and Advances
سال: 2016
ISSN: 2053-2733
DOI: 10.1107/s2053273316099757