Karen G. Fleming
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View article: The lipid bilayer strengthens the cooperative network of membrane proteins
The lipid bilayer strengthens the cooperative network of membrane proteins Open
Membrane proteins fold and function in a lipid bilayer constituting cell membranes. Nonetheless, their structure and function can be recapitulated in diverse amphiphilic assemblies whose compositions deviate from native membranes. It remai…
View article: Phosphoglycerate Kinase Can Adopt a Topologically Misfolded Form that is More Stable than its Native State
Phosphoglycerate Kinase Can Adopt a Topologically Misfolded Form that is More Stable than its Native State Open
The native states of globular proteins are typically viewed as being the most stable conformations on their respective proteins’ soluble free energy landscapes. This view, known as the Thermodynamic Hypothesis, explains why many proteins c…
View article: Advancing Primary Care Coalitions and Cultivating a People-Centered Healthcare System with SCOPE
Advancing Primary Care Coalitions and Cultivating a People-Centered Healthcare System with SCOPE Open
Primary Care is widely acknowledged as the cornerstone for authentic system integration in healthcare (Ontario Ministry of Health, 2022). Historically, however, collaboration with Primary Care has been hampered by fragmentation due to the …
View article: Iron‐Histidine Coordination in Cytochrome b5: A Local Vibrational Mode Study
Iron‐Histidine Coordination in Cytochrome b5: A Local Vibrational Mode Study Open
For a series of cytochrome b5 proteins isolated from various species, including bacteria, animals, and humans, we analyzed the intrinsic strength of their distal/proximal FeN bonds and the intrinsic stiffness of their axial NFeN bond angle…
View article: Exclusive Breastfeeding Rates Upon Hospital Discharge at a Tertiary Centre Prior to and During the COVID-19 Pandemic
Exclusive Breastfeeding Rates Upon Hospital Discharge at a Tertiary Centre Prior to and During the COVID-19 Pandemic Open
This study aimed to describe exclusive breastfeeding (EBF) rates at discharge at Sunnybrook Health Sciences Centre and explore factors that contributed to changes in breastfeeding rates during the COVID-19 pandemic. Overall, 4762 patient c…
View article: The Molecular Basis for Hydrodynamic Properties of PEGylated Human Serum Albumin
The Molecular Basis for Hydrodynamic Properties of PEGylated Human Serum Albumin Open
Polyethylene glycol conjugation provides a protective modification that enhances the pharmacokinetics and solubility of proteins for therapeutic use. A knowledge of the structural ensemble of these PEGylated proteins is necessary to unders…
View article: Membrane defects as a generalized driving force for membrane protein interactions
Membrane defects as a generalized driving force for membrane protein interactions Open
Redirection and acceleration of technological change through policy intervention is essential for addressing climate change and other sustainability challenges. We offer frameworks to conceptualize and model ex ante how local interventions…
View article: Integration of hospital with congregate care homes in response to the COVID-19 pandemic
Integration of hospital with congregate care homes in response to the COVID-19 pandemic Open
The outcomes for older adults residing in congregate care homes improved steadily throughout the COVID-19 pandemic. While this finding is multifactorial, integration with a local hospital partner supported key interventions known to protec…
View article: <scp>FkpA</scp> enhances membrane protein folding using an extensive interaction surface
<span>FkpA</span> enhances membrane protein folding using an extensive interaction surface Open
Outer membrane protein (OMP) biogenesis in gram‐negative bacteria is managed by a network of periplasmic chaperones that includes SurA, Skp, and FkpA. These chaperones bind unfolded OMPs (uOMPs) in dynamic conformational ensembles to suppr…
View article: A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu
A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu Open
The journey by which proteins navigate their energy landscapes to their native structures is complex, involving (and sometimes requiring) many cellular factors and processes operating in partnership with a given polypeptide chain’s intrins…
View article: FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface
FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface Open
Outer membrane protein (OMP) biogenesis in gram-negative bacteria is managed by a network of periplasmic chaperones that includes SurA, Skp, and FkpA. These chaperones bind unfolded OMPs (uOMPs) in dynamic conformational ensembles to suppr…
View article: Generation of Unfolded Outer Membrane Protein Ensembles Targeted by Hydrodynamic Properties
Generation of Unfolded Outer Membrane Protein Ensembles Targeted by Hydrodynamic Properties Open
Outer membrane proteins (OMPs) must exist as an unfolded ensemble while interacting with a chaperone network in the periplasm of Gram-negative bacteria. Here, we developed a method to model unfolded OMP (uOMP) conformational ensembles usin…
View article: Revisiting Macromolecular Hydration with HullRadSAS
Revisiting Macromolecular Hydration with HullRadSAS Open
Hydration of biological macromolecules is important for their stability and function. Historically, attempts have been made to describe the degree of macromolecular hydration using a single parameter over a narrow range of values. Here, we…
View article: 24 A feasibility pilot session: teaching kitchens as innovative nutrition education tool for family medicine residents
24 A feasibility pilot session: teaching kitchens as innovative nutrition education tool for family medicine residents Open
Background The 2006 Canadian Clinical Practice Guidelines on the Management and Prevention of Obesity underscore the importance of nutritional assessment and dietary intervention. Several studies have indicated that medical students receiv…
View article: A Proteome-Wide Map of Chaperone-Assisted Protein Refolding in the Cytosol
A Proteome-Wide Map of Chaperone-Assisted Protein Refolding in the Cytosol Open
The journey by which proteins navigate their energy landscapes to their native structures is complex, involving (and sometimes requiring) many cellular factors and processes operating in partnership with a given polypeptide chain’s intrins…
View article: De novo design of transmembrane β barrels
De novo design of transmembrane β barrels Open
Building a barrel Computational design offers the possibility of making proteins with customized structures and functions. The range of accessible protein scaffolds has expanded with the design of increasingly complex cytoplasmic proteins …
View article: Local Bilayer Hydrophobicity Modulates Membrane Protein Stability
Local Bilayer Hydrophobicity Modulates Membrane Protein Stability Open
Through the insertion of nonpolar side chains into the bilayer, the hydrophobic effect has long been accepted as a driving force for membrane protein folding. However, how the changing chemical composition of the bilayer affects the magnit…
View article: <i>De novo</i>design of transmembrane β-barrels
<i>De novo</i>design of transmembrane β-barrels Open
The ability of naturally occurring transmembrane β-barrel proteins (TMBs) to spontaneously insert into lipid bilayers and form stable transmembrane pores is a remarkable feat of protein evolution and has been exploited in biotechnology for…
View article: SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins
SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins Open
Significance Outer membrane proteins play critical roles in bacterial physiology and increasingly are exploited as antibiotic targets. SurA is the most important chaperone in the OMP biogenesis network and is thought to initiate their fold…
View article: Local Bilayer Hydrophobicity Modulates Membrane Protein Stability
Local Bilayer Hydrophobicity Modulates Membrane Protein Stability Open
Through the insertion of nonpolar side chains into the bilayer, the hydrophobic effect has long been accepted as a driving force for membrane protein folding. However, how the changing chemical composition of the bilayer affects the magnit…
View article: Domain interactions determine the conformational ensemble of the periplasmic chaperone <scp>SurA</scp>
Domain interactions determine the conformational ensemble of the periplasmic chaperone <span>SurA</span> Open
SurA is thought to be the most important periplasmic chaperone for outer membrane protein (OMP) biogenesis. Its structure is composed of a core region and two peptidylprolyl isomerase domains, termed P1 and P2, connected by flexible linker…
View article: Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy
Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy Open
The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side‐chain dynamics of the α‐helical sensory rhodopsin II and the β‐barrel outer membrane protein W have been…