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Journal Abstract Search

5700 related items for PubMed ID: 11580255

  • 1. 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
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  • 3. Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c: 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102.
    Qu K, Vaughn JL, Sienkiewicz A, Scholes CP, Fetrow JS.
    Biochemistry; 1997 Mar 11; 36(10):2884-97. PubMed ID: 9062118
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  • 5. 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
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  • 6. Kinetic barriers to the folding of horse cytochrome C in the reduced state.
    Bhuyan AK, Kumar R.
    Biochemistry; 2002 Oct 22; 41(42):12821-34. PubMed ID: 12379125
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  • 10. Cytochrome c(553), a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics.
    Guidry J, Wittung-Stafshede P.
    J Mol Biol; 2000 Aug 25; 301(4):769-73. PubMed ID: 10966783
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  • 11. Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.
    Godbole S, Hammack B, Bowler BE.
    J Mol Biol; 2000 Feb 11; 296(1):217-28. PubMed ID: 10656828
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  • 12. Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c(551) from Pseudomonas aeruginosa.
    Gianni S, Travaglini-Allocatelli C, Cutruzzolà F, Bigotti MG, Brunori M.
    J Mol Biol; 2001 Jun 22; 309(5):1177-87. PubMed ID: 11399087
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  • 13. Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2.
    Sauder JM, MacKenzie NE, Roder H.
    Biochemistry; 1996 Dec 24; 35(51):16852-62. PubMed ID: 8988024
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  • 14. Equilibrium and kinetic folding of hen egg-white lysozyme under acidic conditions.
    Sasahara K, Demura M, Nitta K.
    Proteins; 2002 Dec 01; 49(4):472-82. PubMed ID: 12402357
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  • 15. Structural characterization of an equilibrium unfolding intermediate in cytochrome c.
    Latypov RF, Cheng H, Roder NA, Zhang J, Roder H.
    J Mol Biol; 2006 Mar 31; 357(3):1009-25. PubMed ID: 16473367
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  • 16. An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core.
    Park SH, O'Neil KT, Roder H.
    Biochemistry; 1997 Nov 25; 36(47):14277-83. PubMed ID: 9400366
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  • 17. Kinetics of folding of the IgG binding domain of peptostreptococcal protein L.
    Scalley ML, Yi Q, Gu H, McCormack A, Yates JR, Baker D.
    Biochemistry; 1997 Mar 18; 36(11):3373-82. PubMed ID: 9116017
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  • 18. Protein folding in classical perspective: folding of horse cytochrome c.
    Bhuyan AK, Rao DK, Prabhu NP.
    Biochemistry; 2005 Mar 01; 44(8):3034-40. PubMed ID: 15723547
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  • 19. Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy.
    Mizuguchi M, Arai M, Ke Y, Nitta K, Kuwajima K.
    J Mol Biol; 1998 Mar 01; 283(1):265-77. PubMed ID: 9761689
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  • 20. A lysine 73-->histidine variant of yeast iso-1-cytochrome c: evidence for a native-like intermediate in the unfolding pathway and implications for m value effects.
    Godbole S, Dong A, Garbin K, Bowler BE.
    Biochemistry; 1997 Jan 07; 36(1):119-26. PubMed ID: 8993325
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