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Journal Abstract Search

211 related items for PubMed ID: 9714163

  • 1. Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions.
    Bhuyan AK, Udgaonkar JB.
    Proteins; 1998 Aug 01; 32(2):241-7. PubMed ID: 9714163
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  • 2. 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. Two structural subdomains of barstar detected by rapid mixing NMR measurement of amide hydrogen exchange.
    Bhuyan AK, Udgaonkar JB.
    Proteins; 1998 Feb 15; 30(3):295-308. PubMed ID: 9517545
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  • 4. Hydrogen exchange behavior of [U-15N]-labeled oxidized and reduced iso-1-cytochrome c.
    Baxter SM, Fetrow JS.
    Biochemistry; 1999 Apr 06; 38(14):4493-503. PubMed ID: 10194371
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  • 5. Protein stability parameters measured by hydrogen exchange.
    Bai Y, Milne JS, Mayne L, Englander SW.
    Proteins; 1994 Sep 06; 20(1):4-14. PubMed ID: 7824522
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  • 11. Direct evidence for the cooperative unfolding of cytochrome c in lipid membranes from H-(2)H exchange kinetics.
    Pinheiro TJ, Cheng H, Seeholzer SH, Roder H.
    J Mol Biol; 2000 Nov 03; 303(4):617-26. PubMed ID: 11054296
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  • 14. Hydrogen exchange in ribonuclease A and ribonuclease S: evidence for residual structure in the unfolded state under native conditions.
    Neira JL, Sevilla P, Menéndez M, Bruix M, Rico M.
    J Mol Biol; 1999 Jan 15; 285(2):627-43. PubMed ID: 9878434
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  • 19. NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding.
    Alexandrescu AT, Jaravine VA, Dames SA, Lamour FP.
    J Mol Biol; 1999 Jun 18; 289(4):1041-54. PubMed ID: 10369781
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