Srinivas, VR and ReddY, GBhanuprakash and Ahmad, Nisar and Swaminathan, Chittoor P and Mitra, Nivedita and Surolia, Avadhesha (2001) Legume lectin family, the 'natural mutants of the quaternary state' provide insights into the relationship between protein stability and oligomerization. In: Biochimica Et Biophysica Acta-General Subjects, 1527 (3). pp. 102-111.
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Legume lectins family of proteins, despite having the same `jelly roll' tertiary structural fold at monomeric level, exhibit considerable variation in their quaternary tructure arising out of small changes in their sequence. Nevertheless, their folding behavior and stability correlates very well with their patterns of assembly into dimers and tetramers. A conservation of their fold during evolution, its wide distribution in many protein families together with the availability of structural information on them make them interesting as proteins to explore the effect of inter- versus intra-subunit interactions in the stability of multimeric proteins. Additionally, as `natural mutants' of quaternary association, proteins of legume lectin family provide interesting paradigms for studies addressing the effect of subunit oligomerization on the stability, folding and function as well as the evolution of multimeric structures.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Keywords:||legume lectins;protein stability;DSC;quaternary structure;subunit interaction;evolution of lectin oligomerization.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||31 Aug 2009 08:29|
|Last Modified:||19 Sep 2010 04:55|
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