Predicting protein–protein interactions from the molecular to the proteome level

O Keskin, N Tuncbag, A Gursoy - Chemical reviews, 2016 - ACS Publications
Identification of protein–protein interactions (PPIs) is at the center of molecular biology
considering the unquestionable role of proteins in cells. Combinatorial interactions result in …

A review of methods available to estimate solvent-accessible surface areas of soluble proteins in the folded and unfolded states

S Ausaf Ali, M Imtaiyaz Hassan, A Islam… - Current Protein and …, 2014 - benthamdirect.com
Solvent accessible surface area (SASA) of proteins has always been considered as a
decisive factor in protein folding and stability studies. It is defined as the surface …

The FTMap family of web servers for determining and characterizing ligand-binding hot spots of proteins

D Kozakov, LE Grove, DR Hall, T Bohnuud… - Nature protocols, 2015 - nature.com
FTMap is a computational map** server that identifies binding hot spots of
macromolecules—ie, regions of the surface with major contributions to the ligand-binding …

Capturing non-local interactions by long short-term memory bidirectional recurrent neural networks for improving prediction of protein secondary structure, backbone …

R Heffernan, Y Yang, K Paliwal, Y Zhou - Bioinformatics, 2017 - academic.oup.com
Motivation The accuracy of predicting protein local and global structural properties such as
secondary structure and solvent accessible surface area has been stagnant for many years …

Phosphorylation in protein-protein binding: effect on stability and function

H Nishi, K Hashimoto, AR Panchenko - Structure, 2011 - cell.com
Posttranslational modifications offer a dynamic way to regulate protein activity, subcellular
localization, and stability. Here we estimate the effect of phosphorylation on protein binding …

Flex ddG: Rosetta ensemble-based estimation of changes in protein–protein binding affinity upon mutation

KA Barlow, S Ó Conchúir, S Thompson… - The Journal of …, 2018 - ACS Publications
Computationally modeling changes in binding free energies upon mutation (interface ΔΔ G)
allows large-scale prediction and perturbation of protein–protein interactions. Additionally …

The role of conformational dynamics and allostery in modulating protein evolution

P Campitelli, T Modi, S Kumar… - Annual review of …, 2020 - annualreviews.org
Advances in sequencing techniques and statistical methods have made it possible not only
to predict sequences of ancestral proteins but also to identify thousands of mutations in the …

SPIDER2: a package to predict secondary structure, accessible surface area, and main-chain torsional angles by deep neural networks

Y Yang, R Heffernan, K Paliwal, J Lyons… - Prediction of protein …, 2017 - Springer
Predicting one-dimensional structure properties has played an important role to improve
prediction of protein three-dimensional structures and functions. The most commonly …

SKEMPI: a structural kinetic and energetic database of mutant protein interactions and its use in empirical models

IH Moal, J Fernández-Recio - Bioinformatics, 2012 - academic.oup.com
Motivation: Empirical models for the prediction of how changes in sequence alter protein–
protein binding kinetics and thermodynamics can garner insights into many aspects of …

Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM

N Tuncbag, A Gursoy, R Nussinov, O Keskin - Nature protocols, 2011 - nature.com
Prediction of protein-protein interactions at the structural level on the proteome scale is
important because it allows prediction of protein function, helps drug discovery and takes …