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Molecular chaperone functions in protein folding and proteostasis
The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
A nature-inspired approach to reactor and catalysis engineering
MO Coppens - Current Opinion in Chemical Engineering, 2012 - Elsevier
Mechanisms used by biology to solve fundamental problems, such as those related to
scalability, efficiency and robustness could guide the design of innovative solutions to …
scalability, efficiency and robustness could guide the design of innovative solutions to …
Extended surfaces modulate hydrophobic interactions of neighboring solutes
AJ Patel, P Varilly, SN Jamadagni, H Acharya… - Proceedings of the …, 2011 - pnas.org
Interfaces are a most common motif in complex systems. To understand how the presence of
interfaces affects hydrophobic phenomena, we use molecular simulations and theory to …
interfaces affects hydrophobic phenomena, we use molecular simulations and theory to …
Thermodynamics and kinetics of protein folding under confinement
Understanding the effects of confinement on protein stability and folding kinetics is important
for describing protein folding in the cellular environment. We have investigated the effects of …
for describing protein folding in the cellular environment. We have investigated the effects of …
Single-molecule spectroscopy of protein folding in a chaperonin cage
Molecular chaperones are known to be essential for avoiding protein aggregation in vivo,
but it is still unclear how they affect protein folding mechanisms. We use single-molecule …
but it is still unclear how they affect protein folding mechanisms. We use single-molecule …
Calculation of local water densities in biological systems: a comparison of molecular dynamics simulations and the 3D-RISM-KH molecular theory of solvation
Water plays a unique role in all living organisms. Not only is it nature's ubiquitous solvent,
but it also actively takes part in many cellular processes. In particular, the structure and …
but it also actively takes part in many cellular processes. In particular, the structure and …
Polar or apolar—the role of polarity for urea-induced protein denaturation
MC Stumpe, H Grubmüller - PLoS computational biology, 2008 - journals.plos.org
Urea-induced protein denaturation is widely used to study protein folding and stability;
however, the molecular mechanism and driving forces of this process are not yet fully …
however, the molecular mechanism and driving forces of this process are not yet fully …
Reconciling theories of chaperonin accelerated folding with experimental evidence
For the last 20 years, a large volume of experimental and theoretical work has been
undertaken to understand how chaperones like GroEL can assist protein folding in the cell …
undertaken to understand how chaperones like GroEL can assist protein folding in the cell …
Graphene oxide as a protein matrix: influence on protein biophysical properties
G Hernández-Cancel, D Suazo-Dávila… - Journal of …, 2015 - Springer
Background This study provides fundamental information on the influence of graphene
oxide (GO) nanosheets and glycans on protein catalytic activity, dynamics, and thermal …
oxide (GO) nanosheets and glycans on protein catalytic activity, dynamics, and thermal …
The Legionella pneumophila Chaperonin – An Unusual Multifunctional Protein in Unusual Locations
RA Garduño, A Chong, GK Nasrallah… - Frontiers in …, 2011 - frontiersin.org
The Legionella pneumophila chaperonin, high temperature protein B (HtpB), was
discovered as a highly immunogenic antigen, only a few years after the identification of L …
discovered as a highly immunogenic antigen, only a few years after the identification of L …