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Structural Architecture (structural + architecture)

Distribution by Scientific Domains
Chemistry60%

Selected Abstracts

Biomimetic Composites: Protein Localization in Silica Nanospheres Derived via Biomimetic Mineralization (Adv. Funct.

ADVANCED FUNCTIONAL MATERIALS, Issue 18 2010
Mater.
Abstract Lysozyme-templated precipitation of silica synthesized by sol-gel chemistry produces a composite material with antimicrobial properties. This study investigates the structural properties of the composite material that allow for retention of the antimicrobial activity of lysozyme. Scanning (SEM) and transmission (TEM) electron microscopy reveal that the composite has a hierarchical structure composed of quasi-spherical structures (,450 nm diameter), which are in turn composed of closely packed spherical structures of ,8,10 nm in diameter. Using small-angle neutron scattering (SANS) with contrast variation, the scattering signatures of the lysozyme and silica within the composite were separated. It was determined that the lysozyme molecules are spatially correlated in the material and form clusters with colloidal silica particles. The size of the clusters determined by SANS agrees well with the structural architecture observed by TEM. BET analysis revealed that the surface area of the composite is relatively low (4.73 m2/g). However, after removal of the protein by heating to 200 °C, the surface area is increased by ,20%. In addition to demonstrating a well organized sol-gel synthesis which generates a functional material with antimicrobial applications, the analysis and modeling approaches described herein can be used for characterizing a wide range of mesoporous and ultrastructural materials. [source]

Protein Localization in Silica Nanospheres Derived via Biomimetic Mineralization

ADVANCED FUNCTIONAL MATERIALS, Issue 18 2010
Mateus B. Cardoso
Abstract Lysozyme-templated precipitation of silica synthesized by sol-gel chemistry produces a composite material with antimicrobial properties. This study investigates the structural properties of the composite material that allow for retention of the antimicrobial activity of lysozyme. Scanning (SEM) and transmission (TEM) electron microscopy reveal that the composite has a hierarchical structure composed of quasi-spherical structures (,450 nm diameter), which are in turn composed of closely packed spherical structures of ,8,10 nm in diameter. Using small-angle neutron scattering (SANS) with contrast variation, the scattering signatures of the lysozyme and silica within the composite were separated. It was determined that the lysozyme molecules are spatially correlated in the material and form clusters with colloidal silica particles. The size of the clusters determined by SANS agrees well with the structural architecture observed by TEM. BET analysis revealed that the surface area of the composite is relatively low (4.73 m2/g). However, after removal of the protein by heating to 200 °C, the surface area is increased by ,20%. In addition to demonstrating a well organized sol-gel synthesis which generates a functional material with antimicrobial applications, the analysis and modeling approaches described herein can be used for characterizing a wide range of mesoporous and ultrastructural materials. [source]

The structure of receptor-associated protein (RAP)

PROTEIN SCIENCE, Issue 8 2007
Donghan Lee
Abstract The receptor-associated protein (RAP) is a molecular chaperone that binds tightly to certain newly synthesized LDL receptor family members in the endoplasmic reticulum (ER) and facilitates their delivery to the Golgi. We have adopted a divide-and-conquer strategy to solve the structures of the individual domains of RAP using NMR spectroscopy. We present here the newly determined structure of domain 2. Based on this structure and the structures of domains 1 and 3, which were solved previously, we utilized experimental small-angle neutron scattering (SANS) data and a novel simulated annealing protocol to characterize the overall structure of RAP. The results reveal that RAP adopts a unique structural architecture consisting of three independent three-helix bundles that are connected by long and flexible linkers. The flexible linkers and the quasi-repetitive structural architecture may allow RAP to adopt various possible conformations when interacting with the LDL receptors, which are also made of repetitive substructure units. [source]

Characterization of Amyloid Fibrils of Human ,-2-Microglobulin by High-Resolution Magic-Angle Spinning NMR

CHEMBIOCHEM, Issue 13 2010
Lukasz Skora Dr.
It's a kind of magic: By using high-resolution magic-angle spinning NMR spectroscopy in combination with hydrogen/deuterium exchange measurements we have shown that at least 18 residues at the N and C termini of ,-2-microglobulin aggregated into amyloid fibrils retain a large degree of mobility occurring on different timescales. This study provides insight into the structural architecture of amyloid fibrils of human ,-2-microglobulin. [source]

Phenylnannolones A,C: Biosynthesis of New Secondary Metabolites from the Myxobacterium Nannocystis exedens

CHEMBIOCHEM, Issue 18 2008
Birgit Ohlendorf
Abstract Myxobacteria are gliding bacteria that belong to the ,-Proteobacteria and are known for their unique biosynthetic capabilities. Among myxobacteria, Nannocystis spp. are most closely related to marine myxobacteria and their secondary metabolism has hardly been investigated. Phenylnannolones A (1), B (2) and C (3) were obtained from a culture of Nannocystis exedens that was isolated from the intertidal region of Crete. Compound 1 had inhibitory activity toward the ABCB1 gene product P-glycoprotein and reversed daunorubicin resistance in cultured cancer cells. Phenylnannolone A has an unusual structural architecture; it is composed of an ethyl-substituted polyene chain linked to a pyrone moiety on one side and to a phenyl ring on the other. The investigation of the biosynthesis with labelled precursors revealed acetate, butyrate and phenylalanine as building blocks for 1. The labelling pattern suggested novel biochemical reactions for the biosynthesis of the starter unit. [source]