Pillai M, Jha S
ACS Omega. 2024; 9(39):40286-40297.
PMID: 39372031
PMC: 11447851.
DOI: 10.1021/acsomega.4c04119.
Wand A
Nature. 2024; 632(8026):741-742.
PMID: 39143275
DOI: 10.1038/d41586-024-02242-7.
Kocher C, Dill K
Proc Natl Acad Sci U S A. 2024; 121(34):e2315000121.
PMID: 39133848
PMC: 11348307.
DOI: 10.1073/pnas.2315000121.
Skrbic T, Giacometti A, Hoang T, Maritan A, Banavar J
Biomolecules. 2024; 14(7).
PMID: 39062519
PMC: 11274641.
DOI: 10.3390/biom14070805.
Faran M, Ray D, Nag S, Raucci U, Parrinello M, Bisker G
J Chem Theory Comput. 2024; 20(13):5428-5438.
PMID: 38924770
PMC: 11238538.
DOI: 10.1021/acs.jctc.4c00464.
Protein folding as a jamming transition.
Grigas A, Liu Z, Logan J, Shattuck M, OHern C
ArXiv. 2024; .
PMID: 38800654
PMC: 11118678.
On the role of native contact cooperativity in protein folding.
Wang D, Frechette L, Best R
Proc Natl Acad Sci U S A. 2024; 121(22):e2319249121.
PMID: 38776371
PMC: 11145220.
DOI: 10.1073/pnas.2319249121.
A Perspective on Protein Structure Prediction Using Quantum Computers.
Doga H, Raubenolt B, Cumbo F, Joshi J, DiFilippo F, Qin J
J Chem Theory Comput. 2024; 20(9):3359-3378.
PMID: 38703105
PMC: 11099973.
DOI: 10.1021/acs.jctc.4c00067.
Residue-based correlation between equilibrium and rate constants is an experimental formulation of the consistency principle for smooth structural changes of proteins.
Kohda D, Hayashi S, Fujinami D
Biophys Physicobiol. 2024; 20(4):e200046.
PMID: 38344030
PMC: 10850467.
DOI: 10.2142/biophysico.bppb-v20.0046.
Folding pathway of a discontinuous two-domain protein.
Agam G, Barth A, Lamb D
Nat Commun. 2024; 15(1):690.
PMID: 38263337
PMC: 10805907.
DOI: 10.1038/s41467-024-44901-3.
Protein folding rate evolution upon mutations.
Vila J
Biophys Rev. 2023; 15(4):661-669.
PMID: 37681091
PMC: 10480377.
DOI: 10.1007/s12551-023-01088-z.
Origins of life: first came evolutionary dynamics.
Kocher C, Dill K
QRB Discov. 2023; 4:e4.
PMID: 37529034
PMC: 10392681.
DOI: 10.1017/qrd.2023.2.
The "Beacon" Structural Model of Protein Folding: Application for Trp-Cage in Water.
Sun Q, He X, Fu Y
Molecules. 2023; 28(13).
PMID: 37446826
PMC: 10343236.
DOI: 10.3390/molecules28135164.
RNA folding pathways from all-atom simulations with a variationally improved history-dependent bias.
Lazzeri G, Micheletti C, Pasquali S, Faccioli P
Biophys J. 2023; 122(15):3089-3098.
PMID: 37355771
PMC: 10432211.
DOI: 10.1016/j.bpj.2023.06.012.
Protein folding mechanism revealed by single-molecule force spectroscopy experiments.
Sun H, Guo Z, Hong H, Yu P, Xue Z, Chen H
Biophys Rep. 2023; 7(5):399-412.
PMID: 37288103
PMC: 10233387.
DOI: 10.52601/bpr.2021.210024.
Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity.
Anderson D, Jayanthi L, Gosavi S, Meiering E
Front Mol Biosci. 2023; 10:1021733.
PMID: 36845544
PMC: 9945329.
DOI: 10.3389/fmolb.2023.1021733.
Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein.
Hong H, Guo Z, Sun H, Yu P, Su H, Ma X
Commun Chem. 2023; 4(1):156.
PMID: 36697724
PMC: 9814876.
DOI: 10.1038/s42004-021-00592-1.
Protein folding problem: enigma, paradox, solution.
Finkelstein A, Bogatyreva N, Ivankov D, Garbuzynskiy S
Biophys Rev. 2023; 14(6):1255-1272.
PMID: 36659994
PMC: 9842845.
DOI: 10.1007/s12551-022-01000-1.
Theoretical Tools to Quantify Stochastic Fluctuations in Single-Molecule Catalysis by Enzymes and Nanoparticles.
Singh D, Punia B, Chaudhury S
ACS Omega. 2023; 7(51):47587-47600.
PMID: 36591158
PMC: 9798497.
DOI: 10.1021/acsomega.2c06316.
Effects of External Perturbations on Protein Systems: A Microscopic View.
Dutta P, Roy P, Sengupta N
ACS Omega. 2022; 7(49):44556-44572.
PMID: 36530249
PMC: 9753117.
DOI: 10.1021/acsomega.2c06199.
