000			02684nam a22001937a 4500
082			_a572.6 _bK185I
100			_aKarmakar, Anurupa _945534
245			_aInvestigating and assessing the role of sequence motifs AXXXA and GXXXG in protein QS Stability _cby Anurupa Karmakar
260			_aIIT Jodhpur _bDepartment of Bioscience and Bioengineering _c2023
300			_a24p. _bHB
500			_aProtein structure and function are critical components of cellular processes, and understanding the molecular mechanisms that regulate these processes is essential for developing new therapeutic interventions for protein-related diseases. The AXXXA and GXXXG motifs are important structural elements found in both membrane and globular proteins, playing diverse roles in regulating protein-protein interactions, stability, and function. These motifs are helical in nature and significantly contribute to the overall structure and function of proteins. In membrane proteins, the AXXXA motif is crucial for the formation and maintenance of protein oligomers, while the GXXXG motif facilitates the formation of transmembrane dimers and oligomers. The CX-O interaction, involving a covalent bond between a cysteine residue and an oxygen atom, is more prevalent than previously understood and has been linked to protein stability, folding, and function. Similarly, in globular proteins, the AXXXA and GXXXG motifs participate in protein-protein interactions, stability, and folding. The AXXXA motif acts as a hinge region allowing conformational changes, while the GXXXG motif contributes to the specificity of protein-protein interactions and the formation of dimers and oligomers. The helical nature of these motifs enables them to induce membrane curvature and regulate lipid-protein interactions in membrane proteins. In globular proteins, these motifs facilitate the formation of protein-protein interfaces and regulate conformational changes. Investigating the AXXXA and GXXXG motifs, along with the CX-O interaction, provides a comprehensive understanding of the molecular mechanisms underlying protein structure and function in both membrane and globular proteins. This research has significant implications for developing new therapeutics, biomaterials, and designing drug delivery systems. Keywords: protein-protein interaction; homodimers and heterodimers; helical motifs; gene ontology analysis
650			_aDepartment of Bioscience and Bioengineering _945535
650			_aProtein-protein interaction _945536
650			_aHelical motifs _945537
650			_aGlobular proteins _945538
650			_aMTech Theses _945539
700			_aDey, Sucharita _945540
942			_cTH
999			_c16602 _d16602