1,721,086 research outputs found
Structural analysis of the β-subunit of the translation initiation factor aIF2 from different species: Role of Zn ions
No full textThe translation initiation factor aIF2 belongs to the aIF-2-beta/ aIF-5 family which is active in the early steps of protein synthesis by forming a ternary complex with GTP and the initiator tRNA. It is involved in the delivery of Met-tRNAiMet to the 40S ribosomal subunit. The solution structure of the intact β-subunit of aIF2 from Sulfolobus solfataricus has been solved by 1H NMR and results composed of an unfolded N-terminus and a folded core domain with four α-helices and three β-strands. The comparison of this structure with the protein of the same family, that we reported here, suggested that that Zn ions can be useful for the correct folding of the C-terminus portion. Starting from this evidence, here we also report a structural homology calculation. The comparison between the Zn-free and Zn-bound forms suggests a possible structure of the terminal region β-subunit of aIF2 from S. solfataricus in presence of Zn
Light-harvesting proteins intermolecular order in the Langmuir-Blodgett (LB) nanofilms – methods and applications.
No full textSpecial Issue on Protein Nanotechnology for Biophysical and Biomedical Studies – Introduction
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Langmuir–Blodgett nanotemplates for protein crystallography
No full textT he new generation of synchrotrons and microfocused beamlines has enabled great progress in X-ray protein crystallography, resulting in new 3D atomic structures for proteins of high interest to the pharmaceutical industry and life sciences. It is, however, often still challenging to produce protein crystals of sufficient size and quality (order, intensity of diffraction, radiation stability). In this protocol, we provide instructions for performing the LangmuirBlodgett (LB) nanotemplate method, a crystallization approach that can be used for any protein (including membrane proteins). We describe how to produce highly ordered 2D LB protein monolayers at the airwater interface and deposit them on glass slides. LB-film formation can be observed by surface-pressure measurements and Brewster angle microscopy (BAM), although its quality can be characterized by atomic force microscopy (AFM) and nanogravimetry. Such films are then used as a 2D template for triggering 3D protein crystal formation by hanging-drop vapor diffusion. The procedure for forming the 2D template takes a few minutes. Structural information about the protein reorganization in the LB film during the crystallization process on the nano level can be obtained using an in situ submicron GISASAXS (grazing-incidence small-angle X-ray scattering) method. MicroGISASAXS spectra, measured directly at the interface of the LB films and protein solution in real time, as described in this protocol, can be interpreted in terms of the buildup of layers, islands, or holes. In our experience, the obtained LB crystals take 110 d to prepare and they are more ordered and radiation stable as compared with those produced using other crystallization methods
Langmuir-Blodgett Protein Multilayer Nanofilms by XFEL
No full textSerial femtosecond crystallography (SFX) at X-ray free electron lasers (XFELs) has created many new opportunities for protein crystallography, including
radiation damage mitigation and the study of dynamics at room temperature. This field is rapidly evolving, requiring new methods of macromolecule organization
into diffracting arrays, since current methods of sample preparation and delivery are often the bottleneck which limits productivity. We propose here the LangmuirBlodgett (LB) protein nanofilm technology as a novel approach for direct “on chip” protein molecules organization into the 3D ordered diffracting arrays. The combination of this advanced technology with the XFEL for fixed target SFX
has the potential to become an important tool for the structure determination of proteins that are difficult to crystallize, such as membrane proteins of life science interest and with pharmaceutical industry impac
Metodo per la crescita accelerata di cristalli proteici su film sottili proteici omologhi
No full textScience and Technology for A Sustainable Human Development
No full textAt the end of the NanoWorld Conference in San Francisco 25 April 2018 it
was decided to formalize the move of the NanoWorld Journal Headquarter from
Texas (USA) at United Scientific Group to Bergamo (Europe) at Fondazione
ELBA Nicolini, moving also to Paris the Nano World Conferences from March
4-6 2019, previously in San Francisco and Boston
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