On the binding affinity of macromolecular interactions: daring to ask why proteins interact

PL Kastritis, AMJJ Bonvin - Journal of The Royal Society …, 2013 - royalsocietypublishing.org
Interactions between proteins are orchestrated in a precise and time-dependent manner,
underlying cellular function. The binding affinity, defined as the strength of these …

Approaches to the description and prediction of the binding affinity of small‐molecule ligands to macromolecular receptors

H Gohlke, G Klebe - Angewandte Chemie International Edition, 2002 - Wiley Online Library
The influence of a xenobiotic compound on an organism is usually summarized by the
expression biological activity. If a controlled, therapeutically relevant, and regulatory action …

[HTML][HTML] Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations

R Guerois, JE Nielsen, L Serrano - Journal of molecular biology, 2002 - Elsevier
We have developed a computer algorithm, FOLDEF (for FOLD-X energy function), to provide
a fast and quantitative estimation of the importance of the interactions contributing to the …

Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding

JK Myers, C Nick Pace, J Martin Scholtz - Protein Science, 1995 - Wiley Online Library
Denaturant m values, the dependence of the free energy of unfolding on denaturant
concentration, have been collected for a large set of proteins. The m value correlates very …

Dual-emitting nanoscale temperature sensors

EJ McLaurin, LR Bradshaw, DR Gamelin - Chemistry of Materials, 2013 - ACS Publications
Soluble luminescent temperature probes are promising candidates for optical thermometry
and thermography applications requiring precise, passive, and spatially resolved …

Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition

I Jelesarov, HR Bosshard - Journal of molecular recognition, 1999 - Wiley Online Library
The principles of isothermal titration calorimetry (ITC) and differential scanning calorimetry
(DSC) are reviewed together with the basic thermodynamic formalism on which the two …

Isothermal titration calorimetry of protein–protein interactions

MM Pierce, CS Raman, BT Nall - Methods, 1999 - Elsevier
The interaction of biologicalmacromolecules, whether protein–DNA, antibody–antigen,
hormone–receptor, etc., illustrates the complexity and diversity of molecular recognition. The …

Protein structure and the energetics of protein stability

AD Robertson, KP Murphy - Chemical reviews, 1997 - ACS Publications
The tendency of proteins to spontaneously adopt a well-defined conformation in solution has
intrigued investigators for many decades. 1 The key questions in the study of this …

Energetics of protein structure

GI Makhatadze, PL Privalov - Advances in protein chemistry, 1995 - Elsevier
Publisher Summary This chapter summarizes the experimental information on protein
energetics. This field is developing fast and the concept of the energetics of protein structure …

Thermodynamic characterization of polypeptide complex coacervation

D Priftis, N Laugel, M Tirrell - Langmuir, 2012 - ACS Publications
The interactions between a series of oppositely charged polypeptide pairs are probed using
isothermal titration calorimetry (ITC) in combination with turbidity measurements and optical …