Investigating and assessing the role of sequence motifs AXXXA and GXXXG in protein QS Stability (Record no. 16602)

MARC details
000 -LEADER
fixed length control field 02684nam a22001937a 4500
082 ## - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 572.6
Item number K185I
100 ## - MAIN ENTRY--AUTHOR NAME
Personal name Karmakar, Anurupa
245 ## - TITLE STATEMENT
Title Investigating and assessing the role of sequence motifs AXXXA and GXXXG in protein QS Stability
Statement of responsibility, etc by Anurupa Karmakar
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Place of publication IIT Jodhpur
Name of publisher Department of Bioscience and Bioengineering
Year of publication 2023
300 ## - PHYSICAL DESCRIPTION
Number of Pages 24p.
Other physical details HB
500 ## - GENERAL NOTE
General note Protein 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.<br/><br/>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.<br/><br/>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.<br/><br/>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.<br/><br/>Keywords: protein-protein interaction; homodimers and heterodimers; helical motifs; gene ontology analysis
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term Department of Bioscience and Bioengineering
Topical Term Protein-protein interaction
Topical Term Helical motifs
Topical Term Globular proteins
Topical Term MTech Theses
700 ## - ADDED ENTRY--PERSONAL NAME
Personal name Dey, Sucharita
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type Thesis
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Withdrawn status Lost status Damaged status Not for loan Collection code Permanent Location Current Location Shelving location Date acquired Source of acquisition Full call number Accession Number Price effective from Koha item type
        Theses S. R. Ranganathan Learning Hub S. R. Ranganathan Learning Hub Reference 2024-04-01 Office of Academics 572.6 K185I TM00538 2024-07-01 Thesis