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2017-06-29
15:03
[PUBDB-2017-06408] Contribution to a book
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Advances in Small- and Wide-Angle X-ray Scattering SAXS and WAXS of Proteins
Encyclopedia of Analytical Chemistry / Meyers, Robert A. (Editor) ; Chichester, UK : John Wiley & Sons, Ltd, , ; ISBN: 9780471976707 ; doi:10.1002/9780470027318.a9447
Encyclopedia of Analytical Chemistry / Meyers, Robert A. (Editor) ; Chichester, UK : John Wiley & Sons, Ltd, , ; ISBN: 9780471976707 ; doi:10.1002/9780470027318.a9447
Chichester, UK : John Wiley & Sons, Ltd, --- (2017) [10.1002/9780470027318.a9447]  GO
Small-angle scattering of X-rays (SAXS) is an established method for low-resolution structural characterization of native biological macromolecules in solution. Recent progress in instrumentation (most notably, high brilliance synchrotron sources) and novel data analysis methods significantly enhanced the capabilities of the technique for the structure research. [...]

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2017-06-29
11:28
[PUBDB-2017-06382] Journal Article
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Structure and activation of C1, the complex initiating the classical pathway of the complement cascade
ddc:000
The complement system is an important antimicrobial and inflammation-generating component of the innate immune system. The classical pathway of complement is activated upon binding of the 774-kDa C1 complex, consisting of the recognition molecule C1q and the tetrameric protease complex C1r2s2, to a variety of activators presenting specific molecular patterns such as IgG- and IgM-containing immune complexes. [...]
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2017-06-29
10:32
[PUBDB-2017-06374] Journal Article
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Uridine as a new scavenger for synchrotron-based structural biology techniques
ddc:540
Macromolecular crystallography (MX) and small-angle X-ray scattering (SAXS) studies on proteins at synchrotron light sources are commonly limited by the structural damage produced by the intense X-ray beam. Several effects, such as aggregation in protein solutions and global and site-specific damage in crystals, reduce the data quality or even introduce artefacts that can result in a biologically misguiding structure. [...]
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2017-06-29
09:29
[PUBDB-2017-06373] Journal Article
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Structure Formation of Binary Blends of Amphiphilic Block Copolymers in Solution and in Bulk
ddc:540
The self-assembly and structure formation in binary blends of asymmetric polystyrene-block-poly(4-vinylpyridine) diblock copolymers in different solvent systems and the bulk morphology of the blend films are studied by using dynamic light scattering, small-angle X-ray scattering, and transmission electron microscopy. In dilute solutions, the chains of pure diblock copolymers or binary blends of diblock copolymers having similar or different molecular weights remain as unimers, form common micelles in selective solvents or form unimers in coexistence with micelles in slightly selective solvents or solvent mixtures. [...]
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2017-06-29
09:19
[PUBDB-2017-06372] Journal Article
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The severe impact of in vivo-like microfluidic flow and the influence of gemini surfactants on amyloid aggregation of hen egg white lysozyme

RSC Advances 7(18), 10973 - 10984 (2017) [10.1039/C6RA26675D]  GO
ddc:540
The formation of amyloid plaques is being intensively studied, as this process underlies severe human diseases, including Alzheimer's disease, and the exact mechanism of this specific aggregation has not been resolved yet. The investigation of its formation is accompanied by the search for substances inhibiting this aggregation process. [...]
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2017-06-23
13:59
[PUBDB-2017-06002] Journal Article
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Thermoresponsive behavior of poly(N-isopropylacrylamide)s with dodecyl and carboxyl terminal groups in aqueous solution: pH-dependent cloud point temperature
ddc:540
It was recently reported that poly(N-isopropyl acrylamide) (PNIPAm) polymers synthesized by RAFT polymerization using S-1-dodecyl-S′-(α,α′-dimethyl-α′′-acetic acid)trithiocarbonate as a chain transfer agent form micelles in aqueous solutions with the core of hydrophobic terminal dodecyl groups and the corona of PNIPAm chains with carboxylic groups at the periphery, the ionization of which prevents the micelles from phase separation above the lower critical solution temperature of PNIPAm in water (Langmuir 30:7986–7992). In this paper, we study the pH- and ionic strength-dependence of the aggregation behavior of two HOOC-PNIPAm-C12 polymers, differing in the degree of polymerization, in aqueous solutions. [...]
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2017-06-23
13:37
[PUBDB-2017-05998] Journal Article
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Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function
ddc:570
Phosducin (Pdc) is a conserved phosphoprotein that, when unphosphorylated, binds with high affinity to the complex of βγ-subunits of G protein transducin (Gtβγ). The ability of Pdc to bind to Gtβγ is inhibited through its phosphorylation at S54 and S73 within the N-terminal domain (Pdc-ND) followed by association with the scaffolding protein 14-3-3. [...]

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2017-06-23
13:36
OpenAccess [PUBDB-2017-05996] Journal Article
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Crystallographic and SAXS studies of S -adenosyl- L -homocysteine hydrolase from Bradyrhizobium elkanii

IUCrJ 4(3), 271 - 282 (2017) [10.1107/S2052252517002433]  GO
ddc:530
S-Adenosyl-L-homocysteine hydrolase (SAHase) from the symbiotic bacterium Bradyrhizobium elkanii (BeSAHase) was crystallized in four ligand complexes with (i) mixed adenosine (Ado) and cordycepin (Cord; 3′-deoxyadenosine), (ii) adenine (Ade), (iii) Ado and (iv) mixed 2′-deoxyadenosine (2′-dAdo) and Ade. The crystal structures were solved at resolutions of 1.84, 1.95, 1.95 and 1.54 Å, respectively. [...]
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2017-06-23
13:21
[PUBDB-2017-05995] Journal Article
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SAXS and other spectroscopic analysis of 12S cruciferin isolated from the seeds of Brassica nigra
ddc:610
Oilseeds of the plant family Brassicaceae are important for providing both lipid and protein contents to human nutrition. Cruciferins (12S globulins) are seed storage proteins, which are getting attention due to their allergenic and pathogenicity related nature. [...]
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2017-06-23
12:01
[PUBDB-2017-05974] Journal Article
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Significance of Individual Residues at the Regulatory Site of Yeast Pyruvate Decarboxylase for Allosteric Substrate Activation

Biochemistry 56(9), 1285 - 1298 (2017) [10.1021/acs.biochem.6b01158]  GO
ddc:570
The catalytic activity of the allosteric enzyme pyruvate decarboxylase from yeast is strictly controlled by its own substrate pyruvate via covalent binding at a separate regulatory site. Kinetic studies, chemical modifications, cross-linking, small-angle X-ray scattering, and crystal structure analyses have led to a detailed understanding of the substrate activation mechanism at an atomic level with C221 as the core moiety of the regulatory site. [...]

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