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Articles by F. Khan
Total Records ( 3 ) for F. Khan
  F. Khan and I. Kobayashi
  The aim of this review is documentation of all the possible cleavage mechanisms of restriction endonucleases. The orthodox restriction endonucleases, which are widely used in molecular biology, recognize and cleave DNA at a single palindromic DNA recognition sequence. They show a high sequence and structural diversity. There are several indications about their convergent evolution from different protein families. Hence it is expected that they must show a great diversity in the DNA cleavage reaction mechanisms. They have been divided into subgroups as Type IIP, E, F and S according to their subunit structure and required number of the cleavage sites, but this classification still found to be insufficient due to diversity in the reaction mechanisms among the group members. In this article, a new classification scheme of orthodox restriction enzyme, based on their choice of phosphodiester bond cleavage is presented. A restriction enzyme may bind to one- or two recognition sites thus making available two or four target phosphodiester bonds to its catalytical site/s. Difference in the cleavage of these available phosphodiester bonds have been used as the basis of classification of restriction enzymes. The restriction enzymes have been classified in six groups viz., 1 of 2, 2 of 2, 1 of 4, 1+1 of 4, 2 of 4 and 4 of 4, where, former figure indicates number of cleaved phosphodiester bond and the later is number available phosphodiester bonds.
  F. Khan , S.M. Gaikwad and M.I. Khan
  In this study, thermodynamics of binding of O-glycan (Galβ1→3GalNAcα1→OSer) and the glycoproteins possessing it, viz., fetuin and mucin to A. hirsuta lectin was studied using Surface Plasmon Resonance (SPR). The binding affinities were in the order of asialomucin >mucin>asialofetuin>fetuin>O-glycan and found to increase with increase in valency of the ligand. Unusual for a lectin-ligand interaction, the binding was endothermic and entropically driven and the higher affinity was associated with a large favorable entropy term. The native fetuin and mucin showed lower affinity than their desialylated counterpart. Kinetic analysis of the binding revealed that the difference in the affinity of different ligands was due to different rates of their association, whereas the dissociation rates were similar and showed decrease with temperature. The activation energy of the association process was lower with desialylated glycoproteins than that of sialylated one resulting in their faster association and higher affinity.
  G Mythen , S Walklate and F. Khan

Since the events of 11 September 2001, Muslim minority groups have been subjected to pervasive scrutiny in the United Kingdom. The 7 July 2005 attacks have led to young Muslims’ being party to intensified modes of monitoring, surveillance and intervention by crime and security agencies. The introduction of multiple forms of counter-terrorism regulation by the state has been underpinned by discourses of (in)security, which have defined British Muslims en bloc as a risky, suspect population. Against this wider backdrop, this paper presents the findings from a study investigating the effects of these processes on young British Pakistanis in the North-West of England. Giving voice to these young people, we explore their responses to risk-victimization and articulate the impacts of legal and cultural regulation both on the management of Muslim identities and performances of safety in the public sphere.

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