164 related articles for article (PubMed ID: 31869980)
1. Loop formation and translational diffusion of intrinsically disordered proteins.
Mühle S; Zhou M; Ghosh A; Enderlein J
Phys Rev E; 2019 Nov; 100(5-1):052405. PubMed ID: 31869980
[TBL] [Abstract][Full Text] [Related]
2. Diversity of hydrodynamic radii of intrinsically disordered proteins.
Białobrzewski MK; Klepka BP; Michaś A; Cieplak-Rotowska MK; Staszałek Z; Niedźwiecka A
Eur Biophys J; 2023 Oct; 52(6-7):607-618. PubMed ID: 37831084
[TBL] [Abstract][Full Text] [Related]
3. 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]
4. 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]
5. 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]
6. Translational diffusion of unfolded and intrinsically disordered proteins.
Nesmelova IV; Melnikova DL; Ranjan V; Skirda VD
Prog Mol Biol Transl Sci; 2019; 166():85-108. PubMed ID: 31521238
[TBL] [Abstract][Full Text] [Related]
7. Effects of Sequence Composition, Patterning and Hydrodynamics on the Conformation and Dynamics of Intrinsically Disordered Proteins.
Vovk A; Zilman A
Int J Mol Sci; 2023 Jan; 24(2):. PubMed ID: 36674958
[TBL] [Abstract][Full Text] [Related]
8. Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements.
Leeb S; Danielsson J
Methods Mol Biol; 2020; 2141():285-302. PubMed ID: 32696363
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein.
Langridge TD; Tarver MJ; Whitten ST
Proteins; 2014 Apr; 82(4):668-78. PubMed ID: 24150971
[TBL] [Abstract][Full Text] [Related]
11. Calibrated Langevin-dynamics simulations of intrinsically disordered proteins.
Smith WW; Ho PY; O'Hern CS
Phys Rev E Stat Nonlin Soft Matter Phys; 2014 Oct; 90(4):042709. PubMed ID: 25375525
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.
Perez RB; Tischer A; Auton M; Whitten ST
Proteins; 2014 Dec; 82(12):3373-84. PubMed ID: 25244701
[TBL] [Abstract][Full Text] [Related]
14. Fluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered Proteins.
Majumdar A; Mukhopadhyay S
Methods Enzymol; 2018; 611():347-381. PubMed ID: 30471693
[TBL] [Abstract][Full Text] [Related]
15. Complete Coupled Binding-Folding Pathway of the Intrinsically Disordered Transcription Factor Protein Brinker Revealed by Molecular Dynamics Simulations and Markov State Modeling.
Collins AP; Anderson PC
Biochemistry; 2018 Jul; 57(30):4404-4420. PubMed ID: 29990433
[TBL] [Abstract][Full Text] [Related]
16. Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.
Arai M; Sugase K; Dyson HJ; Wright PE
Proc Natl Acad Sci U S A; 2015 Aug; 112(31):9614-9. PubMed ID: 26195786
[TBL] [Abstract][Full Text] [Related]
17. Perspective: Chain dynamics of unfolded and intrinsically disordered proteins from nanosecond fluorescence correlation spectroscopy combined with single-molecule FRET.
Schuler B
J Chem Phys; 2018 Jul; 149(1):010901. PubMed ID: 29981536
[TBL] [Abstract][Full Text] [Related]
18. Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
Salvi N; Abyzov A; Blackledge M
Prog Nucl Magn Reson Spectrosc; 2017 Nov; 102-103():43-60. PubMed ID: 29157493
[TBL] [Abstract][Full Text] [Related]
19. Sampling Long- versus Short-Range Interactions Defines the Ability of Force Fields To Reproduce the Dynamics of Intrinsically Disordered Proteins.
Mercadante D; Wagner JA; Aramburu IV; Lemke EA; Gräter F
J Chem Theory Comput; 2017 Sep; 13(9):3964-3974. PubMed ID: 28805390
[TBL] [Abstract][Full Text] [Related]
20. Quantifying Protein Disorder through Measures of Excess Conformational Entropy.
Rajasekaran N; Gopi S; Narayan A; Naganathan AN
J Phys Chem B; 2016 May; 120(19):4341-50. PubMed ID: 27111521
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]