151 related articles for article (PubMed ID: 20553732)
1. Design and structure of an equilibrium protein folding intermediate: a hint into dynamical regions of proteins.
Ayuso-Tejedor S; Angarica VE; Bueno M; Campos LA; Abián O; Bernadó P; Sancho J; Jiménez MA
J Mol Biol; 2010 Jul; 400(4):922-34. PubMed ID: 20553732
[TBL] [Abstract][Full Text] [Related]
2. Structural analysis of an equilibrium folding intermediate in the apoflavodoxin native ensemble by small-angle X-ray scattering.
Ayuso-Tejedor S; García-Fandiño R; Orozco M; Sancho J; Bernadó P
J Mol Biol; 2011 Mar; 406(4):604-19. PubMed ID: 21216251
[TBL] [Abstract][Full Text] [Related]
3. Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate.
Campos LA; Bueno M; Lopez-Llano J; Jiménez MA; Sancho J
J Mol Biol; 2004 Nov; 344(1):239-55. PubMed ID: 15504414
[TBL] [Abstract][Full Text] [Related]
4. Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules.
Nabuurs SM; Westphal AH; van Mierlo CP
J Am Chem Soc; 2008 Dec; 130(50):16914-20. PubMed ID: 19053416
[TBL] [Abstract][Full Text] [Related]
5. Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate.
Irún MP; Garcia-Mira MM; Sanchez-Ruiz JM; Sancho J
J Mol Biol; 2001 Mar; 306(4):877-88. PubMed ID: 11243795
[TBL] [Abstract][Full Text] [Related]
6. Native-specific stabilization of flavodoxin by the FMN cofactor: structural and thermodynamical explanation.
Campos LA; Sancho J
Proteins; 2006 May; 63(3):581-94. PubMed ID: 16444751
[TBL] [Abstract][Full Text] [Related]
7. A general approach for detecting folding intermediates from steady-state and time-resolved fluorescence of single-tryptophan-containing proteins.
Laptenok SP; Visser NV; Engel R; Westphal AH; van Hoek A; van Mierlo CP; van Stokkum IH; van Amerongen H; Visser AJ
Biochemistry; 2011 May; 50(17):3441-50. PubMed ID: 21425856
[TBL] [Abstract][Full Text] [Related]
8. Filling small, empty protein cavities: structural and energetic consequences.
Bueno M; Cremades N; Neira JL; Sancho J
J Mol Biol; 2006 May; 358(3):701-12. PubMed ID: 16563433
[TBL] [Abstract][Full Text] [Related]
9. Noncooperative Formation of the off-pathway molten globule during folding of the alpha-beta parallel protein apoflavodoxin.
Nabuurs SM; Westphal AH; van Mierlo CP
J Am Chem Soc; 2009 Feb; 131(7):2739-46. PubMed ID: 19170491
[TBL] [Abstract][Full Text] [Related]
10. Do proteins with similar folds have similar transition state structures? A diffuse transition state of the 169 residue apoflavodoxin.
Bueno M; Ayuso-Tejedor S; Sancho J
J Mol Biol; 2006 Jun; 359(3):813-24. PubMed ID: 16647718
[TBL] [Abstract][Full Text] [Related]
11. Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment.
López-Llano J; Campos LA; Bueno M; Sancho J
J Mol Biol; 2006 Feb; 356(2):354-66. PubMed ID: 16364364
[TBL] [Abstract][Full Text] [Related]
12. A simple simulation model can reproduce the thermodynamic folding intermediate of apoflavodoxin.
Larriva M; Prieto L; Bruscolini P; Rey A
Proteins; 2010 Jan; 78(1):73-82. PubMed ID: 19688823
[TBL] [Abstract][Full Text] [Related]
13. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.
van Mierlo CP; van Dongen WM; Vergeldt F; van Berkel WJ; Steensma E
Protein Sci; 1998 Nov; 7(11):2331-44. PubMed ID: 9827999
[TBL] [Abstract][Full Text] [Related]
14. Underexposed polar residues and protein stabilization.
Ayuso-Tejedor S; Abián O; Sancho J
Protein Eng Des Sel; 2011 Jan; 24(1-2):171-7. PubMed ID: 20937603
[TBL] [Abstract][Full Text] [Related]
15. The native-state ensemble of proteins provides clues for folding, misfolding and function.
Cremades N; Sancho J; Freire E
Trends Biochem Sci; 2006 Sep; 31(9):494-6. PubMed ID: 16870449
[TBL] [Abstract][Full Text] [Related]
16. Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.
Steensma E; van Mierlo CP
J Mol Biol; 1998 Sep; 282(3):653-66. PubMed ID: 9737928
[TBL] [Abstract][Full Text] [Related]
17. Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation.
Campos LA; Garcia-Mira MM; Godoy-Ruiz R; Sanchez-Ruiz JM; Sancho J
J Mol Biol; 2004 Nov; 344(1):223-37. PubMed ID: 15504413
[TBL] [Abstract][Full Text] [Related]
18. One-state downhill versus conventional protein folding.
Ferguson N; Schartau PJ; Sharpe TD; Sato S; Fersht AR
J Mol Biol; 2004 Nov; 344(2):295-301. PubMed ID: 15522284
[TBL] [Abstract][Full Text] [Related]
19. Thermal unfolding of Apo and Holo Desulfovibrio desulfuricans flavodoxin: cofactor stabilizes folded and intermediate states.
Muralidhara BK; Wittung-Stafshede P
Biochemistry; 2004 Oct; 43(40):12855-64. PubMed ID: 15461458
[TBL] [Abstract][Full Text] [Related]
20. Residue-specific analysis of frustration in the folding landscape of repeat beta/alpha protein apoflavodoxin.
Stagg L; Samiotakis A; Homouz D; Cheung MS; Wittung-Stafshede P
J Mol Biol; 2010 Feb; 396(1):75-89. PubMed ID: 19913555
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]