Protein Structure
Protein Structure
Protein Structure
Presented by
Sonjoy paul
Roll:35
Dhaka International University
Protein structure
Proteins are dynamic molecules that can adopt different conformations, or shapes,
depending on their environment and interactions. Conformational changes are
essential for proteins to carry out their functions effectively.
Conformational Changes
Title text addition
Ligand Binding: When a protein binds to a ligand (such as a substrate,
hormone, or inhibitor), it often undergoes conformational changes. These
changes can involve small adjustments in the positions of amino acids or
larger-scale movements of protein domains.
Conformational changes in proteins
Allosteric Regulation: Some proteins have allosteric sites separate from their active sites.
Binding of a molecule to these allosteric sites can induce conformational changes that affect the
protein's activity at the active site.
Temperature and pH: Changes in temperature or pH can alter the stability and conformation
of proteins. High temperatures or extreme pH levels can denature proteins, causing them to
unfold and lose their function.
Post-translational Modifications: Proteins can undergo post-translational modifications
such as phosphorylation, or acetylation, which can induce conformational changes. These
modifications can affect protein-protein interactions, enzyme activity, and cellular signaling
pathways.
Protein Folding: Newly synthesized proteins often need to fold into their correct three-
dimensional structures to become functional. This process involves conformational changes as
the protein chain rearranges itself to achieve the lowest energy state.
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