Assembly structure of proteins and antimicrobial peptides and their interaction with lipid bilayers
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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| Title |
Assembly structure of proteins and antimicrobial peptides and their interaction with lipid bilayers
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| Creator |
Das, Swagata
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| Subject |
Structural Biology & Bioinformatics
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| Description |
Proteins exist as functional monomers as well as in different multimeric units. Oligomerization is a chemical process that converts monomers to macromolecular complexes through assembly formation involving a finite degree of polymerization. Assembly structures vary from tetramer, hexamers, decamers etc. to oligomers, protofibrils and more complex fibrillar structures. Protein multimers and unidentified oligomers differ in several structural and/or functional aspects. Different attributes of the assembly formations of proteins constitute the central theme of my research and the thesis encompasses the observations related to the structural/conformational perturbation of the protein assemblies of different classes in the presence of different biomimetic environments. Assembly structures of proteins contribute to executing general functions of the cells and are often related to diseases. Antimicrobial peptides co-operatively accomplish functions whereas diseased proteins like beta amyloid peptides amalgamate to render diseased protein assemblies termed as oligomers/fibrils. Several other proteins like adenosine kinase (from Leishmania donovani), tend to aggregate naturally or selectively in presence of ADP, leading to inactivation. The self formed aggregates are of amorphous nature whereas the induced (in presence of ADP) aggregates are of amyloid nature. To propagate the idea of oligomerization in a specific direction emphasizing on the single fluorophore tyrosine, we aimed to study the conformational orientations of the Aβ peptides and purothionin (an AMP from wheat) in micellar environment and other biomimetic environments. The ordered aggregation or fibril formation in globular proteins either exists as oligomers in native state or due to the unfolding of the native state into an intermediate state which is amyloidogenic in nature. We have extended our research to study the sequence complexity of amyloidogenic regions/ aggregation prone regions in intrinsically disordered proteins from different databases (DisProt+IDEAL). Protein sequences are composed of amyloidogenic region(s) (AR) and low complexity region(s) (LCR), both of which play a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR which is present in intrinsically disordered human proteins. Thus the investigation of the structural features of the assembly structures of proteins is critical in understanding the structural and functional aspects of proteins.
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| Date |
2016-09-07
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| Type |
Thesis
NonPeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/2551/1/Thesis_Swagata_Das_2016.pdf
Das, Swagata (2016) Assembly structure of proteins and antimicrobial peptides and their interaction with lipid bilayers. PhD thesis, C U. |
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| Relation |
http://www.eprints.iicb.res.in/2551/
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