Gul S - Search Results

1

Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis.

Gul S, Sonkaria S, Pinitglang S, Florez-Alvarez J, Hussain S, Thomas EW, Ostler EL, Gallacher G, Resmini M, Brocklehurst K. Gul S, et al. Biochem J. 2003 Dec 15;376(Pt 3):813-21. doi: 10.1042/BJ20030716. Biochem J. 2003. PMID: 12946271 Free PMC article.

2

Evidence for 'lock and key' character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes.

Sonkaria S, Boucher G, Flórez-Olvarez J, Said B, Hussain S, Ostler EL, Gul S, Thomas EW, Resmini M, Gallacher G, Brocklehurst K. Sonkaria S, et al. Among authors: gul s. Biochem J. 2004 Jul 1;381(Pt 1):125-30. doi: 10.1042/BJ20031966. Biochem J. 2004. PMID: 15053743 Free PMC article.

3

Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features.

Gul S, Mellor GW, Thomas EW, Brocklehurst K. Gul S, et al. Biochem J. 2006 May 15;396(1):17-21. doi: 10.1042/BJ20051501. Biochem J. 2006. PMID: 16445383 Free PMC article.

4

Determination of the catalytic site content of a polyclonal catalytic antibody preparation.

Resmini M, Gul S, Sonkaria S, Gallacher G, Brocklehurst K. Resmini M, et al. Among authors: gul s. Biochem Soc Trans. 1998 May;26(2):S170. doi: 10.1042/bst026s170. Biochem Soc Trans. 1998. PMID: 9649845 No abstract available.

5

A general kinetic approach to investigation of active-site availability in macromolecular catalysts.

Resmini M, Gul S, Carter S, Sonkaria S, Topham CM, Gallacher G, Brocklehurst K. Resmini M, et al. Among authors: gul s. Biochem J. 2000 Feb 15;346 Pt 1(Pt 1):117-25. Biochem J. 2000. PMID: 10657247 Free PMC article.

6

Ionization characteristics and chemical influences of aspartic acid residue 158 of papain and caricain determined by structure-related kinetic and computational techniques: multiple electrostatic modulators of active-centre chemistry.

Noble MA, Gul S, Verma CS, Brocklehurst K. Noble MA, et al. Among authors: gul s. Biochem J. 2000 Nov 1;351 Pt 3(Pt 3):723-33. Biochem J. 2000. PMID: 11042128 Free PMC article.

7

Generation of nucleophilic character in the Cys25/His159 ion pair of papain involves Trp177 but not Asp158.

Gul S, Hussain S, Thomas MP, Resmini M, Verma CS, Thomas EW, Brocklehurst K. Gul S, et al. Biochemistry. 2008 Feb 19;47(7):2025-35. doi: 10.1021/bi702126p. Epub 2008 Jan 29. Biochemistry. 2008. PMID: 18225918

8

Identification of interactions involved in the generation of nucleophilic reactivity and of catalytic competence in the catalytic site Cys/His ion pair of papain.

Hussain S, Khan A, Gul S, Resmini M, Verma CS, Thomas EW, Brocklehurst K. Hussain S, et al. Among authors: gul s. Biochemistry. 2011 Dec 13;50(49):10732-42. doi: 10.1021/bi201207z. Epub 2011 Nov 17. Biochemistry. 2011. PMID: 22044167

9

Sensitivities of transition state geometries to P1-P2 binding in reactions of papain and actinidin.

Gul S, Pinitglang S, Thomas EW, Verma C, Brocklehurst K. Gul S, et al. Biochem Soc Trans. 1998 May;26(2):S171. doi: 10.1042/bst026s171. Biochem Soc Trans. 1998. PMID: 9649846 No abstract available.

10

Evidence from activation parameters for enzyme active centre desolvation promoted by specific binding interactions.

Mellor GW, Thomas MP, Gul S, Noble MA, Thomas EW, Brocklehurst K. Mellor GW, et al. Among authors: gul s. Biochem Soc Trans. 1994 May;22(2):213S. doi: 10.1042/bst022213s. Biochem Soc Trans. 1994. PMID: 7958275 No abstract available.

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