Nanoworld Institute Fondazione ELBA Nicolini, Pradalunga, Bergamo 24100, Italy; Biophysics and Nanobiotechnology Laboratories, Department of Experimental Medicine, University of Genova, Genoa 16121-16167, Italy; European Synchrotron Radiation Facility.
Published: June 2015
AI Article Synopsis
Article Abstract
A full-atom structure of a protein provides an important piece of information for molecular biologists, but has to be complemented by further knowledge concerning its conformational mobility and functional properties. Some scholars have proposed to integrate proteomics-derived data (mainly obtained with techniques like X-ray and NMR crystallography) with protein bioinformatics and computational approaches, above all molecular dynamics (MD), in order to gain better elucidations about proteins. MD simulations have been applied to different areas of protein sciences, but so far few efforts have been made to couple MD with an understanding of the different crystallization techniques that have been proposed during the decades, like classical vapor diffusion hanging drop and its variants (such as sitting drop), in space- and LB (Langmuir-Blodgett)-based crystallization procedures. Using MD, we show here that the optimal protein crystallization techniques prove to be significantly those based on the LB nanotemplate and on space when compared to the classical vapour diffusion hanging drop and its variants.
Antimicrobial resistance is a significant cause of mortality globally due to infections, a trend that is expected to continue to rise. As existing treatments fail and new drug discovery slows, the urgency to develop novel antimicrobial therapeutics grows stronger. One promising strategy involves targeting bacterial systems exclusive to pathogens, such as the transcription regulator protein GabR.
D-Allulose 3-epimerase catalyzes C-3 epimerization between D-fructose and D-allulose was found in strain M30. The enzyme gene was cloned, and its recombinant enzyme and the mutant variants were expressed in Using the information of the sequence and model structure, we succeed in the improvement of melting temperature for the enzyme without significant loss of the enzyme activity by protein engineering method. The melting temperatures were increased by 2.
The use of green fluorescence protein (GFP) has advanced numerous areas of life sciences. An ultra-thermostable GFP (TGP), engineered from a coral GFP, offers potential advantages over traditional jellyfish-derived GFP because of its high stability. However, owing to its later discovery, TGP lacks the extensive toolsets available for GFP, such as heavy chain-only antibody binders known as nanobodies.
The present study introduces a minimalistic and cost-effective approach to synthesising Gold nanoparticles (AuNPs) using aqueous leaf extracts of Andrographis paniculata. In this synthesis, bioactive metabolites in the leaf extract act as reducing agents, converting Au³⁺ ions to metallic Au⁰, while proteins in the extract form a stabilising layer around the nanoparticles to prevent agglomeration and maintain particle size stability. The synthesised AuNPs were systematically characterised using a range of analytical techniques.
Dipeptides were constructed using hydrophobic amino acid residues following AMP prediction. After that Boc-modification was performed on the screened peptides and finally Boc-Phe-Trp-OMe and Boc-Trp-Trp-OMe were synthesized. Even though no inhibition zones were observed in agar well diffusion assays, minimum inhibitory concentration (MIC) analysis revealed anti-bacterial activity against both Gram-positive and Gram-negative bacteria, with MIC ranging from 230 to 400 μg/mL.
