The relevance of short peptides for an understanding of unfolded and intrinsically disordered proteins

R Schweitzer-Stenner - Physical Chemistry Chemical Physics, 2023 - pubs.rsc.org
Over the last thirty years the unfolded state of proteins has attracted considerable interest
owing to the discovery of intrinsically disordered proteins which perform a plethora of …

Casein and casein micelle structures, functions and diversity in 20 species

C Holt - International Dairy Journal, 2016 - Elsevier
Primary structures of caseins from 20 species, including two monotremes and two
marsupials, have been compared. Sequences of the mature proteins are very divergent …

Conformational manifold sampled by two short linear motif segments probed by circular dichroism, vibrational, and nuclear magnetic resonance spectroscopy

R Schweitzer-Stenner, R Kurbaj, N O'Neill… - Biochemistry, 2023 - ACS Publications
Disordered protein segments called short linear motifs (SLiM) serve as recognition sites for a
variety of biological processes and act as targeting signals, modification, and ligand binding …

The combined use of amide I bands in polarized Raman, IR, and vibrational dichroism spectra for the structure analysis of peptide fibrils and disordered peptides and …

R Schweitzer‐Stenner - Journal of Raman Spectroscopy, 2021 - Wiley Online Library
Raman spectroscopy is generally a versatile tool to explore the structure of proteins and
peptides in solution. However, in spite of the development of ultraviolet (UV) resonance …

What are the minimal folding seeds in proteins? Experimental and theoretical assessment of secondary structure propensities of small peptide fragments

Z Osifová, T Kalvoda, J Galgonek, M Culka… - Chemical …, 2024 - pubs.rsc.org
Certain peptide sequences, some of them as short as amino acid triplets, are significantly
overpopulated in specific secondary structure motifs in folded protein structures. For …

Do molecular dynamics force fields accurately model Ramachandran distributions of amino acid residues in water?

B Andrews, J Guerra, R Schweitzer-Stenner… - Physical Chemistry …, 2022 - pubs.rsc.org
Molecular dynamics (MD) is a powerful tool for studying intrinsically disordered proteins,
however, its reliability depends on the accuracy of the force field. We assess Amber ff19SB …

Molecular modeling and computational study of the chiral-dependent structures and properties of self-assembling diphenylalanine peptide nanotubes

VS Bystrov, PS Zelenovskiy, AS Nuraeva… - Journal of Molecular …, 2019 - Springer
The structure and properties of diphenylalanine (FF) peptide nanotubes (PNT) based on
phenylalanine were investigated by various molecular modeling methods. The main …

Glycine in water favors the polyproline II state

B Andrews, S Zhang, R Schweitzer-Stenner, B Urbanc - Biomolecules, 2020 - mdpi.com
Conformational preferences of amino acid residues in water are determined by the
backbone and side-chain properties. Alanine is known for its high polyproline II (pPII) …

Real-time quantum dynamics reveals complex, many-body interactions in solvated nanodroplets

MB Oviedo, BM Wong - Journal of chemical theory and …, 2016 - ACS Publications
Electronic excitations in the liquid phase are surprisingly rich and considerably more
complex than either gas-phase or solid-state systems. While the majority of physical and …

Dipole cooperativity and polarization frustration determine the secondary structure distribution of short alanine peptides in water

Y Yuan, F Wang - The Journal of Physical Chemistry B, 2023 - ACS Publications
The physical driving forces for secondary structure preferences of hydrated alanine peptide
are investigated with B3LYP-D3 (BJ) and the adaptive force matching (AFM) method. The …