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Journal Abstract Search

144 related items for PubMed ID: 10388575

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  • 4. Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate.
    Irún MP, Garcia-Mira MM, Sanchez-Ruiz JM, Sancho J.
    J Mol Biol; 2001 Mar 02; 306(4):877-88. PubMed ID: 11243795
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  • 5. Stabilization of apoflavodoxin by replacing hydrogen-bonded charged Asp or Glu residues by the neutral isosteric Asn or Gln.
    Irún MP, Maldonado S, Sancho J.
    Protein Eng; 2001 Mar 02; 14(3):173-81. PubMed ID: 11342714
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  • 6. Role of neighboring FMN side chains in the modulation of flavin reduction potentials and in the energetics of the FMN:apoprotein interaction in Anabaena flavodoxin.
    Nogués I, Campos LA, Sancho J, Gómez-Moreno C, Mayhew SG, Medina M.
    Biochemistry; 2004 Dec 07; 43(48):15111-21. PubMed ID: 15568803
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  • 7. Protonation-state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: bovine chymotrypsinogen A.
    Markley JL, Westler WM.
    Biochemistry; 1996 Aug 27; 35(34):11092-7. PubMed ID: 8780512
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  • 9. Salt-induced stabilization of apoflavodoxin at neutral pH is mediated through cation-specific effects.
    Maldonado S, Irún MP, Campos LA, Rubio JA, Luquita A, Lostao A, Wang R, García-Moreno E B, Sancho J.
    Protein Sci; 2002 May 27; 11(5):1260-73. PubMed ID: 11967382
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  • 10. Protonation behavior of histidine 24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin.
    Geierstanger B, Jamin M, Volkman BF, Baldwin RL.
    Biochemistry; 1998 Mar 24; 37(12):4254-65. PubMed ID: 9521748
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  • 14. 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
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  • 16. 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
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  • 17. A novel serine protease inhibition motif involving a multi-centered short hydrogen bonding network at the active site.
    Katz BA, Elrod K, Luong C, Rice MJ, Mackman RL, Sprengeler PA, Spencer J, Hataye J, Janc J, Link J, Litvak J, Rai R, Rice K, Sideris S, Verner E, Young W.
    J Mol Biol; 2001 Apr 13; 307(5):1451-86. PubMed ID: 11292354
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  • 20. The role of a conserved tyrosine residue in high-potential iron sulfur proteins.
    Iwagami SG, Creagh AL, Haynes CA, Borsari M, Felli IC, Piccioli M, Eltis LD.
    Protein Sci; 1995 Dec 13; 4(12):2562-72. PubMed ID: 8580847
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