132 related articles for article (PubMed ID: 37433228)
1. Combining Experiments and Simulations to Examine the Temperature-Dependent Behavior of a Disordered Protein.
Pesce F; Lindorff-Larsen K
J Phys Chem B; 2023 Jul; 127(28):6277-6286. PubMed ID: 37433228
[TBL] [Abstract][Full Text] [Related]
2. Temperature Dependence of Intrinsically Disordered Proteins in Simulations: What are We Missing?
Jephthah S; Staby L; Kragelund BB; Skepö M
J Chem Theory Comput; 2019 Apr; 15(4):2672-2683. PubMed ID: 30865820
[TBL] [Abstract][Full Text] [Related]
3. Molecular Dynamics Simulations Combined with Nuclear Magnetic Resonance and/or Small-Angle X-ray Scattering Data for Characterizing Intrinsically Disordered Protein Conformational Ensembles.
Chan-Yao-Chong M; Durand D; Ha-Duong T
J Chem Inf Model; 2019 May; 59(5):1743-1758. PubMed ID: 30840442
[TBL] [Abstract][Full Text] [Related]
4. Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins.
Pesce F; Newcombe EA; Seiffert P; Tranchant EE; Olsen JG; Grace CR; Kragelund BB; Lindorff-Larsen K
Biophys J; 2023 Jan; 122(2):310-321. PubMed ID: 36518077
[TBL] [Abstract][Full Text] [Related]
5. Self-Diffusive Properties of the Intrinsically Disordered Protein Histatin 5 and the Impact of Crowding Thereon: A Combined Neutron Spectroscopy and Molecular Dynamics Simulation Study.
Fagerberg E; Lenton S; Nylander T; Seydel T; Skepö M
J Phys Chem B; 2022 Feb; 126(4):789-801. PubMed ID: 35044776
[TBL] [Abstract][Full Text] [Related]
6. Computing, Analyzing, and Comparing the Radius of Gyration and Hydrodynamic Radius in Conformational Ensembles of Intrinsically Disordered Proteins.
Ahmed MC; Crehuet R; Lindorff-Larsen K
Methods Mol Biol; 2020; 2141():429-445. PubMed ID: 32696370
[TBL] [Abstract][Full Text] [Related]
7. Force Field Effects in Simulations of Flexible Peptides with Varying Polyproline II Propensity.
Jephthah S; Pesce F; Lindorff-Larsen K; Skepö M
J Chem Theory Comput; 2021 Oct; 17(10):6634-6646. PubMed ID: 34524800
[TBL] [Abstract][Full Text] [Related]
8. Structural characterization of an intrinsically disordered protein complex using integrated small-angle neutron scattering and computing.
Chen SH; Weiss KL; Stanley C; Bhowmik D
Protein Sci; 2023 Oct; 32(10):e4772. PubMed ID: 37646172
[TBL] [Abstract][Full Text] [Related]
9. Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.
Tomasso ME; Tarver MJ; Devarajan D; Whitten ST
PLoS Comput Biol; 2016 Jan; 12(1):e1004686. PubMed ID: 26727467
[TBL] [Abstract][Full Text] [Related]
10. Molecular Dynamics Simulations of Intrinsically Disordered Proteins: Force Field Evaluation and Comparison with Experiment.
Henriques J; Cragnell C; Skepö M
J Chem Theory Comput; 2015 Jul; 11(7):3420-31. PubMed ID: 26575776
[TBL] [Abstract][Full Text] [Related]
11. Generating Intrinsically Disordered Protein Conformational Ensembles from a Database of Ramachandran Space Pair Residue Probabilities Using a Markov Chain.
Cukier RI
J Phys Chem B; 2018 Oct; 122(39):9087-9101. PubMed ID: 30204435
[TBL] [Abstract][Full Text] [Related]
12. An Efficient Method for Estimating the Hydrodynamic Radius of Disordered Protein Conformations.
Nygaard M; Kragelund BB; Papaleo E; Lindorff-Larsen K
Biophys J; 2017 Aug; 113(3):550-557. PubMed ID: 28793210
[TBL] [Abstract][Full Text] [Related]
13. Comment on the Optimal Parameters to Derive Intrinsically Disordered Protein Conformational Ensembles from Small-Angle X-ray Scattering Data Using the Ensemble Optimization Method.
Sagar A; Jeffries CM; Petoukhov MV; Svergun DI; Bernadó P
J Chem Theory Comput; 2021 Apr; 17(4):2014-2021. PubMed ID: 33725442
[TBL] [Abstract][Full Text] [Related]
14. Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.
English LR; Tilton EC; Ricard BJ; Whitten ST
Proteins; 2017 Feb; 85(2):296-311. PubMed ID: 27936491
[TBL] [Abstract][Full Text] [Related]
15. Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET.
Gomes GW; Krzeminski M; Namini A; Martin EW; Mittag T; Head-Gordon T; Forman-Kay JD; Gradinaru CC
J Am Chem Soc; 2020 Sep; 142(37):15697-15710. PubMed ID: 32840111
[TBL] [Abstract][Full Text] [Related]
16. SAXS-Restrained Ensemble Simulations of Intrinsically Disordered Proteins with Commitment to the Principle of Maximum Entropy.
Hermann MR; Hub JS
J Chem Theory Comput; 2019 Sep; 15(9):5103-5115. PubMed ID: 31402649
[TBL] [Abstract][Full Text] [Related]
17. Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ.
Hicks A; Escobar CA; Cross TA; Zhou HX
Biomolecules; 2020 Jun; 10(6):. PubMed ID: 32585849
[TBL] [Abstract][Full Text] [Related]
18. The Effects of Chain Length on the Structural Properties of Intrinsically Disordered Proteins in Concentrated Solutions.
Fagerberg E; Månsson LK; Lenton S; Skepö M
J Phys Chem B; 2020 Dec; 124(52):11843-11853. PubMed ID: 33337879
[TBL] [Abstract][Full Text] [Related]
19. Utilizing Coarse-Grained Modeling and Monte Carlo Simulations to Evaluate the Conformational Ensemble of Intrinsically Disordered Proteins and Regions.
Cragnell C; Rieloff E; Skepö M
J Mol Biol; 2018 Aug; 430(16):2478-2492. PubMed ID: 29573987
[TBL] [Abstract][Full Text] [Related]
20. Structural Characterization of N-WASP Domain V Using MD Simulations with NMR and SAXS Data.
Chan-Yao-Chong M; Deville C; Pinet L; van Heijenoort C; Durand D; Ha-Duong T
Biophys J; 2019 Apr; 116(7):1216-1227. PubMed ID: 30878202
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
