[HTML][HTML] The extrinsic proteins of Photosystem II

TM Bricker, JL Roose, RD Fagerlund, LK Frankel… - … et Biophysica Acta (BBA …, 2012 - Elsevier
In this review we examine the structure and function of the extrinsic proteins of Photosystem
II. These proteins include PsbO, present in all oxygenic organisms, the PsbP and PsbQ …

Evolution of in silico strategies for protein-protein interaction drug discovery

SJY Macalino, S Basith, NAB Clavio, H Chang, S Kang… - Molecules, 2018 - mdpi.com
The advent of advanced molecular modeling software, big data analytics, and high-speed
processing units has led to the exponential evolution of modern drug discovery and better …

Solvent accessible surface area approximations for rapid and accurate protein structure prediction

E Durham, B Dorr, N Woetzel, R Staritzbichler… - Journal of molecular …, 2009 - Springer
The burial of hydrophobic amino acids in the protein core is a driving force in protein folding.
The extent to which an amino acid interacts with the solvent and the protein core is naturally …

KFC2: a knowledge‐based hot spot prediction method based on interface solvation, atomic density, and plasticity features

X Zhu, JC Mitchell - Proteins: Structure, Function, and …, 2011 - Wiley Online Library
Hot spots constitute a small fraction of protein–protein interface residues, yet they account
for a large fraction of the binding affinity. Based on our previous method (KFC), we present …

Identification of computational hot spots in protein interfaces: combining solvent accessibility and inter-residue potentials improves the accuracy

N Tuncbag, A Gursoy, O Keskin - Bioinformatics, 2009 - academic.oup.com
Motivation: Hot spots are residues comprising only a small fraction of interfaces yet
accounting for the majority of the binding energy. These residues are critical in …

Hot spots in protein–protein interfaces: Towards drug discovery

E Cukuroglu, HB Engin, A Gursoy, O Keskin - Progress in biophysics and …, 2014 - Elsevier
Identification of drug-like small molecules that alter protein–protein interactions might be a
key step in drug discovery. However, it is very challenging to find such molecules that target …

HotPoint: hot spot prediction server for protein interfaces

N Tuncbag, O Keskin, A Gursoy - Nucleic acids research, 2010 - academic.oup.com
The energy distribution along the protein–protein interface is not homogenous; certain
residues contribute more to the binding free energy, called 'hot spots'. Here, we present a …

Enhanced prediction of hot spots at protein-protein interfaces using extreme gradient boosting

H Wang, C Liu, L Deng - Scientific reports, 2018 - nature.com
Identification of hot spots, a small portion of protein-protein interface residues that contribute
the majority of the binding free energy, can provide crucial information for understanding the …

Going the distance for protein function prediction: a new distance metric for protein interaction networks

M Cao, H Zhang, J Park, NM Daniels, ME Crovella… - PloS one, 2013 - journals.plos.org
In protein-protein interaction (PPI) networks, functional similarity is often inferred based on
the function of directly interacting proteins, or more generally, some notion of interaction …

APIS: accurate prediction of hot spots in protein interfaces by combining protrusion index with solvent accessibility

JF **a, XM Zhao, J Song, DS Huang - BMC bioinformatics, 2010 - Springer
Background It is well known that most of the binding free energy of protein interaction is
contributed by a few key hot spot residues. These residues are crucial for understanding the …