Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences
Expected and observed effects of volume exclusion on the free energy of rigid and flexible
macromolecules in crowded and confined systems, and consequent effects of crowding and …
macromolecules in crowded and confined systems, and consequent effects of crowding and …
Folding of glycoproteins: toward understanding the biophysics of the glycosylation code
D Shental-Bechor, Y Levy - Current opinion in structural biology, 2009 - Elsevier
Glycosylation is among the most common post-translational modifications that proteins
undergo that may affect many of their activities. It may also modify the underlying energy …
undergo that may affect many of their activities. It may also modify the underlying energy …
Effect of glycosylation on protein folding: a close look at thermodynamic stabilization
D Shental-Bechor, Y Levy - Proceedings of the National …, 2008 - National Acad Sciences
Glycosylation is one of the most common posttranslational modifications to occur in protein
biosynthesis, yet its effect on the thermodynamics and kinetics of proteins is poorly …
biosynthesis, yet its effect on the thermodynamics and kinetics of proteins is poorly …
GroEL-mediated protein folding: making the impossible, possible
Z Lin, HS Rye - Critical reviews in biochemistry and molecular …, 2006 - Taylor & Francis
Protein folding is a spontaneous process that is essential for life, yet the concentrated and
complex interior of a cell is an inherently hostile environment for the efficient folding of many …
complex interior of a cell is an inherently hostile environment for the efficient folding of many …
Folding while bound to chaperones
S Horowitz, P Koldewey, F Stull… - Current opinion in …, 2018 - Elsevier
Highlights•Certain proteins can fold while bound to chaperones.•Kinetic studies on soluble
systems can reveal folding while bound to chaperones.•Folding while bound to chaperones …
systems can reveal folding while bound to chaperones.•Folding while bound to chaperones …
Confinement effects on the kinetics and thermodynamics of protein dimerization
In the cell, protein complexes form by relying on specific interactions between their
monomers. Excluded volume effects due to molecular crowding would lead to correlations …
monomers. Excluded volume effects due to molecular crowding would lead to correlations …
Protein folding simulations: From coarse‐grained model to all‐atom model
Protein folding is an important and challenging problem in molecular biology. During the last
two decades, molecular dynamics (MD) simulation has proved to be a paramount tool and …
two decades, molecular dynamics (MD) simulation has proved to be a paramount tool and …
Nanopore–protein interactions dramatically alter stability and yield of the native state in restricted spaces
We have studied the stability and the yield of the folded WW domains in a spherical
nanopore to provide insights into the changes in the folding characteristics due to …
nanopore to provide insights into the changes in the folding characteristics due to …
The exclusive effects of chaperonin on the behavior of proteins with 52 knot
The folding of proteins with a complex knot is still an unresolved question. Based on
representative members of Ubiquitin C-terminal Hydrolases (UCHs) that contain the 52 knot …
representative members of Ubiquitin C-terminal Hydrolases (UCHs) that contain the 52 knot …
[HTML][HTML] GroEL assisted folding of large polypeptide substrates in Escherichia coli: present scenario and assignments for the future
Escherichia coli chaperonins GroEL and GroES are indispensable for survival and growth of
the cell since they provide essential assistance to the folding of many newly translated …
the cell since they provide essential assistance to the folding of many newly translated …