K. G. Fleming

The Molecular Basis for Hydrodynamic Properties of PEGylated Human Serum Albumin

The paper uses simulations and HullRad to predict hydrodynamic properties of PEGylated proteins, aiding in the design of modified therapeutics.

Lipid Bilayer Strengthens the Cooperative Network of Membrane Proteins

This study shows that lipid bilayers enhance membrane protein stability and their response to external stimuli by influencing hydrophobic thickness and amphiphile packing.

FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface

This study investigates FkpA's role in enhancing outer membrane protein folding and shows it binds clients with an extensive interface, distinct from other chaperones.

Generation of Unfolded Outer Membrane Protein Ensembles Targeted by Hydrodynamic Properties

The paper models unfolded outer membrane protein ensembles using experimental data and simulations to understand their conformational differences.

Revisiting Macromolecular Hydration with HullRadSAS

The paper introduces a method to calculate two types of macromolecular hydration, surface shell water and entrained water, to better explain hydration-related properties and hydrodynamic behavior.

A Proteome-Wide Map of Chaperone-Assisted Protein Refolding in the Cytosol

This study maps chaperone-assisted protein refolding in E. coli cytosol using mass spectrometry, showing GroEL refolds most proteins and identifies intransigent proteins that fold co-translationally.

Local Bilayer Hydrophobicity Modulates Membrane Protein Stability

The paper determines transfer free energies of nonpolar side chains in membranes using experiments and simulations, revealing a correlation with local water concentration and implications for membrane protein design and disease mutation analysis.

Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy

This study characterizes the fast internal motion and residual conformational entropy of membrane proteins using solution NMR relaxation techniques, revealing unique dynamics compared to soluble proteins.

SurA is a "Groove-y" Chaperone That Expands Unfolded Outer Membrane Proteins

This paper investigates how SurA, a bacterial chaperone, interacts with unfolded outer membrane proteins (uOMPs) using structural biology techniques, revealing distinct binding modes and a mechanism for uOMP expansion.

Protein structure prediction and design in a biologically-realistic implicit membrane

This paper develops an implicit membrane model for protein structure prediction and design, improving accuracy in membrane protein properties and sequence recovery.