Electrostatic interactions in protein structure, folding, binding, and condensation

HX Zhou, X Pang - Chemical reviews, 2018 - ACS Publications
Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …

Unfolded proteins and protein folding studied by NMR

HJ Dyson, PE Wright - Chemical reviews, 2004 - ACS Publications
Preparation of biological macromolecules in the pure state requires that cells be disrupted,
releasing and mixing the contents. Only the most stable and highly structured molecules can …

A summary of the measured pK values of the ionizable groups in folded proteins

GR Grimsley, JM Scholtz, CN Pace - Protein Science, 2009 - Wiley Online Library
We tabulated 541 measured pK values reported in the literature for the Asp, Glu, His, Cys,
Tyr, and Lys side chains, and the C and N termini of 78 folded proteins. The majority of these …

Protein ionizable groups: pK values and their contribution to protein stability and solubility

CN Pace, GR Grimsley, JM Scholtz - Journal of Biological Chemistry, 2009 - ASBMB
The structure, stability, solubility, and function of proteins depend on their net charge and on
the ionization state of the individual residues. Consequently, biochemists are interested in …

Rational engineering of enzyme stability

VGH Eijsink, A Bjørk, S Gåseidnes, R Sirevåg… - Journal of …, 2004 - Elsevier
During the past 15 years there has been a continuous flow of reports describing proteins
stabilized by the introduction of mutations. These reports span a period from pioneering …

Measurement of histidine pKa values and tautomer populations in invisible protein states

AL Hansen, LE Kay - … of the National Academy of Sciences, 2014 - National Acad Sciences
The histidine imidazole side chain plays a critical role in protein function and stability. Its
importance for catalysis is underscored by the fact that histidines are localized to active sites …

Strategies for tailoring pH performances of glycoside hydrolases

SF Li, F Cheng, YJ Wang, YG Zheng - Critical Reviews in …, 2023 - Taylor & Francis
Glycoside hydrolases (GHs) exhibit high activity and stability under harsh conditions, such
as high temperatures and extreme pHs, given their wide use in industrial biotechnology …

Polymer models of protein stability, folding, and interactions

HX Zhou - Biochemistry, 2004 - ACS Publications
The unfolded state and flexible linkers in the folded structure play essential roles in protein
stability and folding and protein− protein interactions. Intrinsic to these roles is the fact that …

Principal component analysis of the pH-dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR

K Sakurai, Y Goto - Proceedings of the National Academy of …, 2007 - National Acad Sciences
To clarify the pH-dependent conformational transitions of proteins, we propose an approach
in which structural changes monitored by heteronuclear sequential quantum correlation …

Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non …

JH Cho, S Sato, DP Raleigh - Journal of molecular biology, 2004 - Elsevier
Comparatively little is known about the role of non-native interactions in protein folding and
their role in both folding and stability is controversial. We demonstrate that non-native …