Protein Structure: How the Proteins are organized in tertiary Structure
This is very compact three-dimensional structure, the wound has previously viewed and secondary structures of the segments without secondary structure. There is also the ionic interactions , the hydrophobic interaction (stronger in the center of the protein), the hydrogen bonds stabilizing folding, the forces Van der Waals, the disulfide bridges.
“In proteins, the spatial arrangement of amino acid residues that are far from each other in the linear sequence, as well as the pattern of hydrogen bonds, disulphide bonds, hydrophobic bonds and ionic bonds”.
- What are the stabilizing forces involved in the Protein organization
- These were created after the completion of three-dimensional protein folding and have a key role in maintaining the tertiary structure .
- The biologically active form of Globular Proteins are in Tertiary structure, which is in three-dimensional conformation.
- The best example of Tertiary Structure of Proteins are Myoglobin (Muscle Respiratory Pigment) and Ribunuclease. (RNA digestive enzyme).
Basic points on Tertiary Structure of Proteins:
The folding of a protein is connects to the Genomic function
- This leads us to define the concept of areas .
- Domains are compact subunits.
- They are linked by peptide sequences usually short and without secondary structure.
- These areas are almost “independent” from the rest of the tertiary structure of the globular protein.
- Indeed, they have their own and are stable tertiary structure independently of the rest of the polypeptide chain.
- There is a specific function of the protein. This introduces the concept of stereo specificity . These areas may appear as topographically crevices, particular areas. This spatial configuration must meet those of other structures of other molecules, dimensional structure, biological role and stereo-specificity therefore are necessarily linked.
- This is what defines active site : the spatial conformation of protein amino acids normally close and distant form the active site, the active site often housed in the crevasse . Thus the observed protein-ligand recognition .
- This recognition is performed by establishment of complementarity then non-covalent bonds that do not require the intervention of a catalyst.