The Interactions Between Proteins and Automating Predictions with Mass Spectrometry
Session Number
Project ID: BIO 16
Advisor(s)
Dr. Kevin Drew, University of Illinois at Chicago
Discipline
Biology
Start Date
17-4-2024 9:20 AM
End Date
17-4-2024 9:35 AM
Abstract
This research aims to explore the impact of local geometric constraints on the conformations of amino acid side-chain dihedral angles in proteins. The understanding of the fundamental principles that govern protein structure is essential for the development of new proteins and the analysis of mutations in natural proteins. Our specific objective is to quantify the influence of geometric and physicochemical properties on the selection of dihedral angle combinations by amino acid side chains in peptides and proteins. Despite significant progress in structural biology, the reasons behind the prevalence of certain side-chain dihedral angle combinations and the scarcity of others remain unclear. Through the use of computational methods and the analysis of protein structures, we aim to unravel the intricate relationship between local geometry and side-chain conformations. This research contributes to the ongoing efforts to enhance our knowledge of protein structure and function, potentially benefiting protein engineering and drug design endeavors.
The Interactions Between Proteins and Automating Predictions with Mass Spectrometry
This research aims to explore the impact of local geometric constraints on the conformations of amino acid side-chain dihedral angles in proteins. The understanding of the fundamental principles that govern protein structure is essential for the development of new proteins and the analysis of mutations in natural proteins. Our specific objective is to quantify the influence of geometric and physicochemical properties on the selection of dihedral angle combinations by amino acid side chains in peptides and proteins. Despite significant progress in structural biology, the reasons behind the prevalence of certain side-chain dihedral angle combinations and the scarcity of others remain unclear. Through the use of computational methods and the analysis of protein structures, we aim to unravel the intricate relationship between local geometry and side-chain conformations. This research contributes to the ongoing efforts to enhance our knowledge of protein structure and function, potentially benefiting protein engineering and drug design endeavors.