Cosolvent effects on protein stability
Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …
solution can easily be altered by the addition of small organic molecules known as …
Disulfide bonds and protein folding
The applications of disulfide-bond chemistry to studies of protein folding, structure, and
stability are reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). After …
stability are reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). After …
The molecular basis for the chemical denaturation of proteins by urea
BJ Bennion, V Daggett - Proceedings of the National …, 2003 - National Acad Sciences
Molecular dynamics simulations of the protein chymotrypsin inhibitor 2 in 8 M urea at 60° C
were undertaken to investigate the molecular basis of chemical denaturation. The protein …
were undertaken to investigate the molecular basis of chemical denaturation. The protein …
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
Pulse field gradient NMR methods have been used to determine the effective hydrodynamic
radii of a range of native and nonnative protein conformations. From these experimental …
radii of a range of native and nonnative protein conformations. From these experimental …
Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
L Hua, R Zhou, D Thirumalai… - Proceedings of the …, 2008 - National Acad Sciences
The mechanism of denaturation of proteins by urea is explored by using all-atom
microseconds molecular dynamics simulations of hen lysozyme generated on BlueGene/L …
microseconds molecular dynamics simulations of hen lysozyme generated on BlueGene/L …
Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
H Lu, B Isralewitz, A Krammer, V Vogel, K Schulten - Biophysical journal, 1998 - cell.com
Abstract Titin, a 1-μm-long protein found in striated muscle myofibrils, possesses unique
elastic and extensibility properties in its I-band region, which is largely composed of a PEVK …
elastic and extensibility properties in its I-band region, which is largely composed of a PEVK …
Theoretical methods for the description of the solvent effect in biomolecular systems
The environment plays a key role in the determination of the properties and reactivity of
substances in condensed phases. The complexity of chemical phenomena in solution has …
substances in condensed phases. The complexity of chemical phenomena in solution has …
Dewetting and hydrophobic interaction in physical and biological systems
Hydrophobicity manifests itself differently on large and small length scales. This review
focuses on large-length-scale hydrophobicity, particularly on dewetting at single …
focuses on large-length-scale hydrophobicity, particularly on dewetting at single …
Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
WK Lim, J Rösgen… - Proceedings of the …, 2009 - National Acad Sciences
The mechanism by which urea and guanidinium destabilize protein structure is
controversial. We tested the possibility that these denaturants form hydrogen bonds with …
controversial. We tested the possibility that these denaturants form hydrogen bonds with …
Steered molecular dynamics investigations of protein function
B Isralewitz, J Baudry, J Gullingsrud, D Kosztin… - Journal of Molecular …, 2001 - Elsevier
Molecular recognition and mechanical properties of proteins govern molecular processes in
the cell that can cause disease and can be targeted for drug design. Single molecule …
the cell that can cause disease and can be targeted for drug design. Single molecule …