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209 related items for PubMed ID: 16846236

  • 1. Stability and folding/unfolding kinetics of the homotrimeric coiled coil Lpp-56.
    Bjelić S, Karshikoff A, Jelesarov I.
    Biochemistry; 2006 Jul 25; 45(29):8931-9. PubMed ID: 16846236
    [Abstract] [Full Text] [Related]

  • 2. Electrostatic contribution to the thermodynamic and kinetic stability of the homotrimeric coiled coil Lpp-56: A computational study.
    Bjelić S, Wieninger S, Jelesarov I, Karshikoff A.
    Proteins; 2008 Feb 15; 70(3):810-22. PubMed ID: 17729276
    [Abstract] [Full Text] [Related]

  • 3. Kinetics and thermodynamics of the unfolding and refolding of the three-stranded alpha-helical coiled coil, Lpp-56.
    Dragan AI, Potekhin SA, Sivolob A, Lu M, Privalov PL.
    Biochemistry; 2004 Nov 30; 43(47):14891-900. PubMed ID: 15554696
    [Abstract] [Full Text] [Related]

  • 4. Folding of horse cytochrome c in the reduced state.
    Bhuyan AK, Udgaonkar JB.
    J Mol Biol; 2001 Oct 05; 312(5):1135-60. PubMed ID: 11580255
    [Abstract] [Full Text] [Related]

  • 5. Kinetically robust monomeric protein from a hyperthermophile.
    Mukaiyama A, Takano K, Haruki M, Morikawa M, Kanaya S.
    Biochemistry; 2004 Nov 02; 43(43):13859-66. PubMed ID: 15504048
    [Abstract] [Full Text] [Related]

  • 6. Extremely fast folding of a very stable leucine zipper with a strengthened hydrophobic core and lacking electrostatic interactions between helices.
    Dürr E, Jelesarov I, Bosshard HR.
    Biochemistry; 1999 Jan 19; 38(3):870-80. PubMed ID: 9893981
    [Abstract] [Full Text] [Related]

  • 7. How do chemical denaturants affect the mechanical folding and unfolding of proteins?
    Cao Y, Li H.
    J Mol Biol; 2008 Jan 04; 375(1):316-24. PubMed ID: 18021802
    [Abstract] [Full Text] [Related]

  • 8. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
    Patra AK, Udgaonkar JB.
    Biochemistry; 2007 Oct 23; 46(42):11727-43. PubMed ID: 17902706
    [Abstract] [Full Text] [Related]

  • 9. A kinetic analysis of the folding and unfolding of OmpA in urea and guanidinium chloride: single and parallel pathways.
    Andersen KK, Wang H, Otzen DE.
    Biochemistry; 2012 Oct 23; 51(42):8371-83. PubMed ID: 22992178
    [Abstract] [Full Text] [Related]

  • 10. Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper).
    Jelesarov I, Dürr E, Thomas RM, Bosshard HR.
    Biochemistry; 1998 May 19; 37(20):7539-50. PubMed ID: 9585569
    [Abstract] [Full Text] [Related]

  • 11. The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus.
    Kaushik JK, Ogasahara K, Yutani K.
    J Mol Biol; 2002 Mar 01; 316(4):991-1003. PubMed ID: 11884137
    [Abstract] [Full Text] [Related]

  • 12. Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: spectroscopic description of the native, intermediate, and unfolded states.
    Nallamsetty S, Dubey VK, Pande M, Ambasht PK, Jagannadham MV.
    Biochimie; 2007 Nov 01; 89(11):1416-24. PubMed ID: 17658212
    [Abstract] [Full Text] [Related]

  • 13. Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants.
    Liu J, Cao W, Lu M.
    J Mol Biol; 2002 May 03; 318(3):877-88. PubMed ID: 12054830
    [Abstract] [Full Text] [Related]

  • 14. The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding.
    Ogasahara K, Nakamura M, Nakura S, Tsunasawa S, Kato I, Yoshimoto T, Yutani K.
    Biochemistry; 1998 Dec 15; 37(50):17537-44. PubMed ID: 9860869
    [Abstract] [Full Text] [Related]

  • 15. Thermodynamic characterization of monomeric and dimeric forms of CcdB (controller of cell division or death B protein).
    Bajaj K, Chakshusmathi G, Bachhawat-Sikder K, Surolia A, Varadarajan R.
    Biochem J; 2004 Jun 01; 380(Pt 2):409-17. PubMed ID: 14763902
    [Abstract] [Full Text] [Related]

  • 16. Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments.
    Godoy-Ruiz R, Ariza F, Rodriguez-Larrea D, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM.
    J Mol Biol; 2006 Oct 06; 362(5):966-78. PubMed ID: 16935299
    [Abstract] [Full Text] [Related]

  • 17. Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase.
    Wani AH, Udgaonkar JB.
    J Mol Biol; 2009 Mar 27; 387(2):348-62. PubMed ID: 19356591
    [Abstract] [Full Text] [Related]

  • 18. Two-state folding of horse ferrocytochrome c: analyses of linear free energy relationship, chevron curvature, and stopped-flow burst relaxation kinetics.
    Kumar R, Bhuyan AK.
    Biochemistry; 2005 Mar 01; 44(8):3024-33. PubMed ID: 15723546
    [Abstract] [Full Text] [Related]

  • 19. Stability and folding mechanism of mesophilic, thermophilic and hyperthermophilic archael histones: the importance of folding intermediates.
    Topping TB, Gloss LM.
    J Mol Biol; 2004 Sep 03; 342(1):247-60. PubMed ID: 15313621
    [Abstract] [Full Text] [Related]

  • 20. Non-linear effects of temperature and urea on the thermodynamics and kinetics of folding and unfolding of hisactophilin.
    Wong HJ, Stathopulos PB, Bonner JM, Sawyer M, Meiering EM.
    J Mol Biol; 2004 Dec 03; 344(4):1089-107. PubMed ID: 15544814
    [Abstract] [Full Text] [Related]

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