Coarse-grained protein models and their applications

S Kmiecik, D Gront, M Kolinski, L Wieteska… - Chemical …, 2016 - ACS Publications
The traditional computational modeling of protein structure, dynamics, and interactions
remains difficult for many protein systems. It is mostly due to the size of protein …

Molecular dynamics simulations: advances and applications

A Hospital, JR Goñi, M Orozco… - … and Applications in …, 2015 - Taylor & Francis
Molecular dynamics simulations have evolved into a mature technique that can be used
effectively to understand macromolecular structure-to-function relationships. Present …

Comparing proteins by their internal dynamics: Exploring structure–function relationships beyond static structural alignments

C Micheletti - Physics of life reviews, 2013 - Elsevier
The growing interest for comparing protein internal dynamics owes much to the realisation
that protein function can be accompanied or assisted by structural fluctuations and …

Large-Scale Conformational Changes and Protein Function: Breaking the in silico Barrier

L Orellana - Frontiers in molecular biosciences, 2019 - frontiersin.org
Large-scale conformational changes are essential to link protein structures with their
function at the cell and organism scale, but have been elusive both experimentally and …

In Silico Strategies in Tuberculosis Drug Discovery

SJY Macalino, JB Billones, VG Organo, MCO Carrillo - Molecules, 2020 - mdpi.com
Tuberculosis (TB) remains a serious threat to global public health, responsible for an
estimated 1.5 million mortalities in 2018. While there are available therapeutics for this …

Prediction and validation of protein intermediate states from structurally rich ensembles and coarse-grained simulations

L Orellana, O Yoluk, O Carrillo, M Orozco… - Nature …, 2016 - nature.com
Protein conformational changes are at the heart of cell functions, from signalling to ion
transport. However, the transient nature of the intermediates along transition pathways …

CABS-flex predictions of protein flexibility compared with NMR ensembles

M Jamroz, A Kolinski, S Kmiecik - Bioinformatics, 2014 - academic.oup.com
Motivation: Identification of flexible regions of protein structures is important for
understanding of their biological functions. Recently, we have developed a fast approach for …

Oncogenic mutations at the EGFR ectodomain structurally converge to remove a steric hindrance on a kinase-coupled cryptic epitope

L Orellana, AH Thorne, R Lema… - Proceedings of the …, 2019 - National Acad Sciences
Epidermal growth factor receptor (EGFR) signaling is initiated by a large ligand-favored
conformational change of the extracellular domain (ECD) from a closed, self-inhibited …

Residues coevolution guides the systematic identification of alternative functional conformations in proteins

P Sfriso, M Duran-Frigola, R Mosca, A Emperador… - Structure, 2016 - cell.com
We present here a new approach for the systematic identification of functionally relevant
conformations in proteins. Our fully automated pipeline, based on discrete molecular …

[HTML][HTML] Thermodynamics and folding landscapes of large proteins from a statistical mechanical model

S Gopi, A Aranganathan, AN Naganathan - Current Research in Structural …, 2019 - Elsevier
Statistical mechanical models that afford an intermediate resolution between macroscopic
chemical models and all-atom simulations have been successful in capturing folding …