252 related articles for article (PubMed ID: 21425856)
1. 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]
2. 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]
3. Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin.
Bollen YJ; Sánchez IE; van Mierlo CP
Biochemistry; 2004 Aug; 43(32):10475-89. PubMed ID: 15301546
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. Apoflavodoxin (un)folding followed at the residue level by NMR.
van Mierlo CP; van den Oever JM; Steensma E
Protein Sci; 2000 Jan; 9(1):145-57. PubMed ID: 10739257
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. 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]
8. 5-fluorotryptophan as dual probe for ground-state heterogeneity and excited-state dynamics in apoflavodoxin.
Visser NV; Westphal AH; Nabuurs SM; van Hoek A; van Mierlo CP; Visser AJ; Broos J; van Amerongen H
FEBS Lett; 2009 Sep; 583(17):2785-8. PubMed ID: 19619543
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of the off-pathway intermediate during apoflavodoxin folding.
Engel R; Westphal AH; Huberts DHEW; Nabuurs SM; Lindhoud S; Visser AJWG; van Mierlo CPM
J Biol Chem; 2008 Oct; 283(41):27383-27394. PubMed ID: 18640986
[TBL] [Abstract][Full Text] [Related]
11. Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.
Visser NV; Westphal AH; van Hoek A; van Mierlo CP; Visser AJ; van Amerongen H
Biophys J; 2008 Sep; 95(5):2462-9. PubMed ID: 18708472
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. 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]
14. Concurrent presence of on- and off-pathway folding intermediates of apoflavodoxin at physiological ionic strength.
Houwman JA; Westphal AH; Visser AJWG; Borst JW; van Mierlo CPM
Phys Chem Chem Phys; 2018 Mar; 20(10):7059-7072. PubMed ID: 29473921
[TBL] [Abstract][Full Text] [Related]
15. The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain.
Sridevi K; Juneja J; Bhuyan AK; Krishnamoorthy G; Udgaonkar JB
J Mol Biol; 2000 Sep; 302(2):479-95. PubMed ID: 10970747
[TBL] [Abstract][Full Text] [Related]
16. Folding of horse cytochrome c in the reduced state.
Bhuyan AK; Udgaonkar JB
J Mol Biol; 2001 Oct; 312(5):1135-60. PubMed ID: 11580255
[TBL] [Abstract][Full Text] [Related]
17. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
van Mierlo CP; Steensma E
J Biotechnol; 2000 May; 79(3):281-98. PubMed ID: 10867188
[TBL] [Abstract][Full Text] [Related]
18. Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants.
Ionescu RM; Eftink MR
Biochemistry; 1997 Feb; 36(5):1129-40. PubMed ID: 9033404
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. 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]
[Next] [New Search]
