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Items: 1 to 20 of 102

1.

Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY.

Shi J, Nobrega RP, Schwantes C, Kathuria SV, Bilsel O, Matthews CR, Lane TJ, Pande VS.

Sci Rep. 2017 Mar 8;7:44116. doi: 10.1038/srep44116.

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 4;406(4):604-19. doi: 10.1016/j.jmb.2010.12.027. Epub 2011 Jan 7.

PMID:
21216251
3.

Folding of proteins with a flavodoxin-like architecture.

Houwman JA, van Mierlo CPM.

FEBS J. 2017 Oct;284(19):3145-3167. doi: 10.1111/febs.14077. Epub 2017 Apr 28. Review.

4.

Direct examination of the relevance for folding, binding and electron transfer of a conserved protein folding intermediate.

Lamazares E, Vega S, Ferreira P, Medina M, Galano-Frutos JJ, Martínez-Júlvez M, Velázquez-Campoy A, Sancho J.

Phys Chem Chem Phys. 2017 Jul 26;19(29):19021-19031. doi: 10.1039/c7cp02606d.

PMID:
28702545
5.

Oligomeric states along the folding pathways of β2-microglobulin: kinetics, thermodynamics, and structure.

Rennella E, Cutuil T, Schanda P, Ayala I, Gabel F, Forge V, Corazza A, Esposito G, Brutscher B.

J Mol Biol. 2013 Aug 9;425(15):2722-36. doi: 10.1016/j.jmb.2013.04.028. Epub 2013 May 3.

PMID:
23648836
6.

Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold.

Bollen YJ, van Mierlo CP.

Biophys Chem. 2005 Apr 22;114(2-3):181-9. Epub 2004 Dec 19.

PMID:
15829351
7.

Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin.

Stagg L, Zhang SQ, Cheung MS, Wittung-Stafshede P.

Proc Natl Acad Sci U S A. 2007 Nov 27;104(48):18976-81. Epub 2007 Nov 16.

8.
9.

Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding.

Korzhnev DM, Kay LE.

Acc Chem Res. 2008 Mar;41(3):442-51. doi: 10.1021/ar700189y. Epub 2008 Feb 15. Review.

PMID:
18275162
10.

Interrupted hydrogen/deuterium exchange reveals the stable core of the remarkably helical molten globule of alpha-beta parallel protein flavodoxin.

Nabuurs SM, van Mierlo CP.

J Biol Chem. 2010 Feb 5;285(6):4165-72. doi: 10.1074/jbc.M109.087932. Epub 2009 Dec 3.

11.

Alternate pathways for folding in the flavodoxin fold family revealed by a nucleation-growth model.

Nelson ED, Grishin NV.

J Mol Biol. 2006 May 5;358(3):646-53. Epub 2006 Mar 3.

PMID:
16563435
12.

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 23;400(4):922-34. doi: 10.1016/j.jmb.2010.05.050. Epub 2010 May 27.

PMID:
20553732
13.

The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9.

Meng W, Luan B, Lyle N, Pappu RV, Raleigh DP.

Biochemistry. 2013 Apr 16;52(15):2662-71. doi: 10.1021/bi301667u. Epub 2013 Apr 4.

PMID:
23480024
14.

Modulation of frustration in folding by sequence permutation.

Nobrega RP, Arora K, Kathuria SV, Graceffa R, Barrea RA, Guo L, Chakravarthy S, Bilsel O, Irving TC, Brooks CL 3rd, Matthews CR.

Proc Natl Acad Sci U S A. 2014 Jul 22;111(29):10562-7. doi: 10.1073/pnas.1324230111. Epub 2014 Jul 7.

15.

Highly Collapsed Conformation of the Initial Folding Intermediates of β-Lactoglobulin with Non-Native α-Helix.

Konuma T, Sakurai K, Yagi M, Goto Y, Fujisawa T, Takahashi S.

J Mol Biol. 2015 Sep 25;427(19):3158-65. doi: 10.1016/j.jmb.2015.07.018. Epub 2015 Jul 30.

PMID:
26232603
16.

The native ensemble and folding of a protein molten-globule: functional consequence of downhill folding.

Naganathan AN, Orozco M.

J Am Chem Soc. 2011 Aug 10;133(31):12154-61. doi: 10.1021/ja204053n. Epub 2011 Jul 15.

PMID:
21732676
17.
18.

Defining the nature of thermal intermediate in 3 state folding proteins: apoflavodoxin, a study case.

García-Fandiño R, Bernadó P, Ayuso-Tejedor S, Sancho J, Orozco M.

PLoS Comput Biol. 2012;8(8):e1002647. doi: 10.1371/journal.pcbi.1002647. Epub 2012 Aug 23.

19.

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 12;344(1):239-55.

PMID:
15504414
20.

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. doi: 10.1002/prot.22521.

PMID:
19688823

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