One of the most important interactions responsible for protein folding and stability are
hydrogen bonds between peptide groups. There is a constant competition between the …

Contrary to the widespread view that hydrogen bonding and its entropy effect play a
dominant role in protein folding, folding into helical and hairpin‐like structures is observed in …

Protein folding is a fascinating, not fully understood phenomenon in biology. Molecular
dynamics (MD) simulations are an invaluable tool to study conformational changes in …

Taking protein G with 56 residues for a case study, we investigate the mechanism of protein
folding. In addition to its native structure possessing α-helix and β-sheet contents of 27 …

In the last decade many advances have been made on molecular dynamics simulations and
different force fields were developed from the combination of differentiable functions of the …

The paper presents a model for simulating the protein folding process in silico. The two-step
model (which consists of the early stage—ES and the late stage—LS) is verified using two …

Computer simulation using molecular dynamics is increasingly used to simulate the folding
equilibria of peptides and small proteins. Yet, the quality of the obtained results depends …

The thermal folding of hydrated lysozyme has been investigated by means of the high
resolution nuclear magnetic resonance (NMR) technique. The proton NMR signal belonging …

The second step in the protein folding process depends on interactions with external force
fields and on an internal field that governs intramolecular interactions. The internal field …

Introduction: The protein folding process is very sensitive to environmental conditions. Many
possibilities in the form of numerous pathways for this process can—if an incorrect one is …