Low-resolution neutron crystallography of biological macromolecules
نویسندگان
چکیده
منابع مشابه
Neutron protein crystallography: beyond the folding structure of biological macromolecules.
Neutron diffraction provides an experimental method of directly locating H atoms in proteins, a technique complementary to ultra-high-resolution X-ray diffraction. Three different types of neutron diffractometers for biological macromolecules have been constructed in Japan, France and the USA, and they have been used to determine the crystal structures of proteins up to resolution limits of 1.5...
متن کاملCrystallography of Biological Macromolecules
Cyclohexene nucleic acids (CeNA) contain a cyclohexene ring instead of the normal -D-2’-deoxyribose. The cyclohexene oligonucleotide GTGTACAC was synthesized using phosphoramidite chemistry and standard protecting groups [1]. CeNA is stable against enzymatic degradation and induces RNaseH activity. CeNA also forms more stable duplexes with RNA than its natural analogues [2] [3]. Crystals of GTG...
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...
متن کاملCrystallography of Biological Macromolecules
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...
متن کاملCrystallography of Biological Macromolecules
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 of Crystallography
سال: 2011
ISSN: 0108-7673
DOI: 10.1107/s0108767311095298