Protein conformational ensembles in function: roles and mechanisms
The sequence-structure-function paradigm has dominated twentieth century molecular
biology. The paradigm tacitly stipulated that for each sequence there exists a single, well …
biology. The paradigm tacitly stipulated that for each sequence there exists a single, well …
Frustration, function and folding
Natural protein molecules are exceptional polymers. Encoded in apparently random strings
of amino-acids, these objects perform clear physical tasks that are rare to find by simple …
of amino-acids, these objects perform clear physical tasks that are rare to find by simple …
Designing multi-epitope vaccine against Staphylococcus aureus by employing subtractive proteomics, reverse vaccinology and immuno-informatics approaches
Staphylococcus aureus is a deadly human bacterial pathogen that causes a wide variety of
clinical manifestations. Invasive S. aureus infections in hospitals and the community are one …
clinical manifestations. Invasive S. aureus infections in hospitals and the community are one …
Predicting protein conformational motions using energetic frustration analysis and AlphaFold2
Proteins perform their biological functions through motion. Although high throughput
prediction of the three-dimensional static structures of proteins has proved feasible using …
prediction of the three-dimensional static structures of proteins has proved feasible using …
Local energetic frustration conservation in protein families and superfamilies
Energetic local frustration offers a biophysical perspective to interpret the effects of
sequence variability on protein families. Here we present a methodology to analyze local …
sequence variability on protein families. Here we present a methodology to analyze local …
Frustration in fuzzy protein complexes leads to interaction versatility
Disordered proteins frequently serve as interaction hubs involving a constrained variety of
partners. Complexes with different partners frequently exhibit distinct binding modes …
partners. Complexes with different partners frequently exhibit distinct binding modes …
Insights into the biased activity of dextromethorphan and haloperidol towards SARS-CoV-2 NSP6: in silico binding mechanistic analysis
The outbreak of novel coronavirus disease 2019 (COVID-19) caused by severe acute
respiratory syndrome coronavirus-2 (SARS-CoV-2) virus continually led to infect a large …
respiratory syndrome coronavirus-2 (SARS-CoV-2) virus continually led to infect a large …
Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR
L Troussicot, A Vallet, M Molin… - Journal of the …, 2023 - ACS Publications
Disulfide bond formation is fundamentally important for protein structure and constitutes a
key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins …
key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins …
Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model
TR Sisk, P Robustelli - … of the National Academy of Sciences, 2024 - National Acad Sciences
A central challenge in the study of intrinsically disordered proteins is the characterization of
the mechanisms by which they bind their physiological interaction partners. Here, we utilize …
the mechanisms by which they bind their physiological interaction partners. Here, we utilize …
Sterically confined rearrangements of SARS-CoV-2 Spike protein control cell invasion
E Dodero-Rojas, JN Onuchic, PC Whitford - Elife, 2021 - elifesciences.org
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is highly contagious, and
transmission involves a series of processes that may be targeted by vaccines and …
transmission involves a series of processes that may be targeted by vaccines and …