These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

147 related items for 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 23; 400(4):922-34. PubMed ID: 20553732
    [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 04; 406(4):604-19. PubMed ID: 21216251
    [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 12; 344(1):239-55. PubMed ID: 15504414
    [Abstract] [Full Text] [Related]

  • 4.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 5.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No 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 05; 358(3):701-12. PubMed ID: 16563433
    [Abstract] [Full Text] [Related]

  • 9.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 10.
    ; . PubMed ID:
    [No 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 17; 356(2):354-66. PubMed ID: 16364364
    [Abstract] [Full Text] [Related]

  • 12.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 13.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 14.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 15.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 16.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 17.
    ; . PubMed ID:
    [No 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 19; 344(2):295-301. PubMed ID: 15522284
    [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 12; 43(40):12855-64. PubMed ID: 15461458
    [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 12; 396(1):75-89. PubMed ID: 19913555
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 8.