Differentiation of Bovine, Porcine, and Fish Gelatins by Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy (ATR-FTIRS) Coupled with Pattern Recognition.

Bovine, porcine, and fish gelatins have been differentiated based on their spectra collected by attenuated total reflectance FTIR spectroscopy (ATR-FTIRS) coupled with pattern recognition. Three tree-based classification methods, a fuzzy rule-building expert system (FuRES), support vector machine classification trees (SVMTreeG and SVMTreeH), and one reference model, super partial least-squares discriminant analysis (sPLS-DA), were evaluated with and without two preprocessing techniques, namely standard normal variate (SNV) and principal component orthogonal signal correction (PC-OSC). Validation of these methods was obtained with 95% confidence intervals with 10 bootstraps and 4 Latin partitions (10:4).

Prediction of total antioxidant activity of Prunella L. species by automatic partial least square regression applied to 2-way liquid chromatographic UV spectral images.

Four different data representations were evaluated for the determination of the total antioxidant activities of four different Prunella L. species, which are Prunella vulgaris, Prunella grandiflora, Prunella laciniata, and Prunella orientalis Bornm. Three different antioxidant assays, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABST), 2,2-diphenyl-1-picrylhydrazyl (DPPH), and Folin-Ciocalteu (FC) reagent measured the total antioxidant activity and phenolic content of the four Prunella L.

Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein.

The E46K genetic missense mutation of the wild-type α-synuclein protein was recently identified in a family of Spanish origin with hereditary Parkinson's disease. Detailed understanding of the structures of the monomeric E46K mutant-type α-synuclein protein as well as the impact of the E46K missense mutation on the conformations and free energy landscapes of the wild-type α-synuclein are required for gaining insights into the pathogenic mechanism of Parkinson's disease. In this study, we use extensive parallel tempering molecular dynamics simulations along with thermodynamic calculations to assess the secondary and tertiary structural properties as well as the conformational preferences of the monomeric wild-type and E46K mutant-type α-synuclein proteins in an aqueous solution environment.

Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics.

The genetic missense A30P mutation of the wild-type α-synuclein protein results in the replacement of the 30th amino acid residue from alanine (Ala) to proline (Pro) and was initially found in the members of a German family who developed Parkinson's disease. Even though the structures of these proteins have been measured before, detailed understanding about the structures and their relationships with free energy landscapes is lacking, which is of interest to provide insights into the pathogenic mechanism of Parkinson's disease. We report the secondary and tertiary structures and conformational free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins in an aqueous solution environment via extensive parallel tempering molecular dynamics simulations along with thermodynamic calculations.