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Shift in nucleotide conformational equilibrium contributes to increased rate of catalysis of GpAp versus GpA in barnase.
Giraldo J, De Maria L, Wodak SJ. Giraldo J, et al. Proteins. 2004 Aug 1;56(2):261-76. doi: 10.1002/prot.20137. Proteins. 2004. PMID: 15211510
The increase in K(M), caused by the presence of additional non-productive binding modes for GpA, should however be counterbalanced by the propensity of free GpA to adopt folded conformations in solution, which are unable to bind the enzyme and by the tighter binding of GpAp (Gira …
The increase in K(M), caused by the presence of additional non-productive binding modes for GpA, should however be counterbalanced by the pr …
SESAM: a relational database for structure and sequence of macromolecules.
Huysmans M, Richelle J, Wodak SJ. Huysmans M, et al. Proteins. 1991;11(1):59-76. doi: 10.1002/prot.340110108. Proteins. 1991. PMID: 1961702
Unfolding simulations of the 85-102 beta-hairpin of barnase.
Pugliese L, Prévost M, Wodak SJ. Pugliese L, et al. J Mol Biol. 1995 Aug 18;251(3):432-47. doi: 10.1006/jmbi.1995.0446. J Mol Biol. 1995. PMID: 7650741
The quaternary structure of carbonmonoxy hemoglobin ypsilanti.
Janin J, Wodak SJ. Janin J, et al. Proteins. 1993 Jan;15(1):1-4. doi: 10.1002/prot.340150102. Proteins. 1993. PMID: 8451234
Effect of nucleotide substrate binding on the pKa of catalytic residues in barnase.
Gordon-Beresford RM, Van Belle D, Giraldo J, Wodak SJ. Gordon-Beresford RM, et al. Proteins. 1996 Jun;25(2):180-94. doi: 10.1002/(SICI)1097-0134(199606)25:2<180::AID-PROT4>3.0.CO;2-M. Proteins. 1996. PMID: 8811734
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