To gain more insight into the physicochemical aspects of a protein structure from the first principles, conformational space of all 8000 "capped" tripeptides (i.e., N-Ac-X 1 X 2 X 3 -NH-CH 3 , where X i is one of the 20 natural amino acids) was investigated computationally. An enormous dataset (denoted P-CONF_1.6M and containing close to 1 600 000 conformers in total) has been obtained by employing a composite protocol combining density functional theory, semiempirical quantum mechanics (SQM), and state-of-theart solvation methods with 1000 K molecular dynamics (MD) used to generate initial structures (200 snapshots for each tripeptide). This allowed us to present the first rigorous QM-based glimpse at the vast conformational space spanned by small protein fragments. The same computational procedure was repeated for tripeptide fragments taken from the SCOPe database of three-dimensional protein folds, by restraining them to their geometry in a protein. Such complementary data allowed us to compare the distribution of conformational strain energies of unrestrained tripeptidic fragments "in solvent" with those in existing protein chains. Besides providing a rigorous (ab initio) proof of a few wellknown concepts and hypotheses concerning protein structures, such as the distribution of (φ, ψ) angles in Ramachandran plots, we have made several observations that came as a certain surprise: (1) distribution of conformational energies does not significantly differ between the "unbiased/unrestrained" conformers obtained from MD sampling in solvent and the biased conformers, i.e., those of a given tripeptide obtained from protein structures; (2) conformational (strain) energy window up to ∼20 to 25 kcal•mol −1 is readily available to tripeptide fragments within the context of a protein chain; (3) overpopulation in certain regions of Ramachandran plot was observed for the unbiased conformers. Last but not least, the massive dataset of accurate (DFT-D3// COSMO-RS) conformational (free) energies of ∼1.6 M peptide conformers, P-CONF_1.6M, obtained throughout this work may serve as excellent dataset for calibrating and benchmarking of popular force fields.

Lead (Pb) is a ubiquitous poisonous metal, affecting the health of vast populations worldwide. Medications to treat Pb poisoning suffer from various limitations and are often toxic owing to insufficient metal selectivity. Here, we report a cyclic tetrapeptide that selectively binds Pb and eradicates its toxic effect on the cellular level, with superior potency than state‐of‐the‐art drugs. The Pb‐peptide complex is remarkably strong and was characterized experimentally and computationally. Accompanied by the lack of toxicity and enhanced stability of this peptide, these qualities indicate its merit as a potential remedy for Pb poisoning.

Context. Meteor spectra are commonly interpreted using data from databases and tables. Several studies have demonstrated very sophisticated calculations of elemental compositions of meteoroid bodies based on the computation of synthetic meteor spectra or on the spectral analysis of airglow plasma containing evaporated, atomized, and ionized meteoroid matter. However, considering accuracy, reliability of computations, lack of laboratory experimental data in this field, as well as the complicated physical structure of meteor plasma, such qualitative assignment or quantitative calculations are still extensively discussed in the scientific community. Even on the laboratory level, many studies have shown the high complexity of the acquisition and interpretation of the data that are recorded with techniques of emission spectroscopy that are in fashion and philosophy similar to the spectral analysis of meteor plasma, that is, detection and quantification of the elements that are ablated from complicated multicomponent matrices. Aims. The current study is focused on the application of terawatt-class laser-induced breakdown spectroscopy (TC-LIBS) of real samples of chondritic meteorites. We recorded emission spectra with high resolution and high precision that contain spectral lines that are typical for real meteoric spectra. Experimental data were compiled in a form that is convenient for the meteoric spectra interpretation and calibration. Methods. TC-LIBS was carried out by a high-power terawatt-class laser facility, the Prague Asterix Laser System (PALS). The spectra were simultaneously recorded by an echelle high-resolution spectrograph in the UV/VIS spectral ranges and by a low-resolution spectrograph that was used for real observation of meteor spectra. We also present calculated synthetic spectra based on data from the NIST atomic spectra database. Results. We assembled etalon qualitative tables of major meteoric spectral features that can be used both for the spectral wavelength calibration of low-resolution observational instruments and for the exact interpretation of meteor spectra. The data are compared with real meteor spectra.

The natural tripeptide glutathione (GSH) is a ubiquitous compound harboring various biological tasks, among them interacting with essential and toxic metal ions. Yet, although weakly binding the poisonous metal lead (Pb), GSH poorly detoxifies it. β-Mercaptoaspartic acid is a new-to-nature novel amino acid that was found to enhance the Pb-detoxification capability of a synthetic cyclic tetrapeptide. Aiming to explore the advantages of noncanonical amino acids (ncAAs) of this nature, we studied the detoxification capabilities of GSH and three analogue peptides, each of which contains at least one ncAA that harbors both free carboxylate and thiolate groups. A thorough investigation that includes in vitro detoxification and mechanistic evaluations, metal-binding affinity, metal selectivity, and computational studies shows that these ncAAs are highly beneficial in additively enhancing Pb binding and reveals the importance of both high affinity and metal selectivity in synergistically reducing Pb toxicity in cells. Hence, such ncAAs join the chemical toolbox against Pb poisoning and pollution, enabling peptides to strongly and selectively bind the toxic metal ion.