ArticleBiophysical journal2010
Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme from experiment and molecular dynamics.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 58 citations in OpenAlex.
- Insights on Aggregation of Hen Egg-White Lysozyme from Raman Spectroscopy and MD Simulations.Molecules (Basel, Switzerland) · 2022Article
- Hydrogen/Deuterium Exchange Behavior During Denaturing/Refolding Processes Determined in Tetragonal Hen Egg-White Lysozyme Crystals.Molecular biotechnology · 2022Article
- Article
- On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy.Molecules (Basel, Switzerland) · 2021Article
- Non-covalent Encapsulation of siRNA with Cell-Penetrating Peptides.Methods in molecular biology (Clifton, N.J.) · 2021Article
- PDBMD2CD: providing predicted protein circular dichroism spectra from multiple molecular dynamics-generated protein structures.Nucleic acids research · 2020Article
- Unfolding Pathways of Hen Egg-White Lysozyme in Ethanol.The journal of physical chemistry. B · 2019Article
- Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle.Science advances · 2018Article
- Article
- Milling solid proteins to enhance activity after melt-encapsulation.International journal of pharmaceutics · 2017Article
- Critical structural fluctuations of proteins upon thermal unfolding challenge the Lindemann criterion.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Reversible thermal unfolding of a yfdX protein with chaperone-like activity.Scientific reports · 2016Article
- Effects of pressure on the dynamics of an oligomeric protein from deep-sea hyperthermophile.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14).Biophysical journal · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 6 institutions in 4 countries.
Funding
Abstract
Synchrotron radiation circular dichroism, Fourier transform infrared, and nuclear magnetic resonance spectroscopies, and small-angle x-ray scattering were used to monitor the reversible thermal unfolding of hen egg white lysozyme. The results were compared with crystal structures and high- and low-temperature structures derived from molecular-dynamics calculations. The results of both experimental and computational methods indicate that the unfolding process starts with the loss of β-structures followed by the reversible loss of helix content from ∼40% at 20°C to 27% at 70°C and ∼20% at 77°C, beyond which unfolding becomes irreversible. Concomitantly there is a reversible increase in the radius of gyration of the protein from 15 Å to 18 Å. The reversible decrease in forward x-ray scattering demonstrates a lack of aggregation upon unfolding, suggesting the change is due to a larger dilation of hydration water than of bulk water. Molecular-dynamics simulations suggest a similar sequence of events and are in good agreement with the (1)H(N) chemical shift differences in nuclear magnetic resonance. This study demonstrates the power of complementary methods for elucidating unfolding/refolding processes and the nature of both the unfolded structure, for which there is no crystallographic data, and the partially unfolded forms of the protein that can lead to fibril formation and disease.
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