Computational Modelling and Bioinformatics Study For Evaluation of Oligomerization of Protein Structures inDifferent Living Species
EMANUAL MICHAEL PATELIA
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Oligomerization of protein plays important role in various proteins function. In this manner, understanding, foreseeing, and, at last, building oligomerization exhibits a long-standing interest. From the viewpoint of structural science, protein–protein interactions have fundamentally been dissected regarding the biophysical nature and development of protein interfaces. Here, my point is to quantify the essentialness of the bigger structural connection of protein interfaces in protein evolution and its cooperation. Specifically, I ask to what degree intersubunit geometry influences oligomerization state. I characterize a set of structural parameters depicting the general geometry and relative positions of interfaces of homomeric complexes with various oligomeric states. This permits us to quantify the commitment of immediate sequence changes in interfaces versus indirect changes outside the interface that influence intersubunit geometry. I found that such indirect or allosteric changes influencing intersubunit geometry through indirect mechanism has equal importance as interface sequence mutation for evolution of oligomeric states of structures.