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 …

Evolutionary biochemistry: revealing the historical and physical causes of protein properties

MJ Harms, JW Thornton - Nature Reviews Genetics, 2013 - nature.com
The repertoire of proteins and nucleic acids in the living world is determined by evolution;
their properties are determined by the laws of physics and chemistry. Explanations of these …

Biophysics of protein evolution and evolutionary protein biophysics

T Sikosek, HS Chan - Journal of The Royal Society …, 2014 - royalsocietypublishing.org
The study of molecular evolution at the level of protein-coding genes often entails comparing
large datasets of sequences to infer their evolutionary relationships. Despite the importance …

Structural and functional constraints in the evolution of protein families

CL Worth, S Gong, TL Blundell - Nature Reviews Molecular Cell Biology, 2009 - nature.com
High-throughput genomic sequencing has focused attention on understanding differences
between species and between individuals. When this genetic variation affects protein …

Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection

F Morcos, NP Schafer, RR Cheng, JN Onuchic… - Proceedings of the …, 2014 - pnas.org
The energy landscape used by nature over evolutionary timescales to select protein
sequences is essentially the same as the one that folds these sequences into functioning …

Protein folding in the cell: challenges and progress

A Gershenson, LM Gierasch - Current opinion in structural biology, 2011 - Elsevier
It is hard to imagine a more extreme contrast than that between the dilute solutions used for
in vitro studies of protein folding and the crowded, compartmentalized, sticky, spatially …

Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions

SL Shammas, TPJ Knowles, AJ Baldwin… - Biophysical journal, 2011 - cell.com
The self-assembly of proteins and peptides into polymeric amyloid fibrils is a process that
has important implications ranging from the understanding of protein misfolding disorders to …
C Rancurel, M Khosravi, AK Dunker… - Journal of …, 2009 - journals.asm.org
It is widely assumed that new proteins are created by duplication, fusion, or fission of
existing coding sequences. Another mechanism of protein birth is provided by overlap** …

Protein thermostability is owing to their preferences to non-polar smaller volume amino acids, variations in residual physico-chemical properties and more salt-bridges

AS Panja, B Bandopadhyay, S Maiti - PloS one, 2015 - journals.plos.org
Introduction Protein thermostability is an important field for its evolutionary perspective of
mesophilic versus thermophilic relationship and for its industrial/therapeutic applications …

[HTML][HTML] Tuning transcriptional regulation through signaling: a predictive theory of allosteric induction

M Razo-Mejia, SL Barnes, NM Belliveau, G Chure… - Cell systems, 2018 - cell.com
Allosteric regulation is found across all domains of life, yet we still lack simple, predictive
theories that directly link the experimentally tunable parameters of a system to its input …