Protein tertiary structure

Amino acid side chains and the backbone may interact and bond in a number of ways.

[3] The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition.

For example, in secreted proteins, which are not bathed in cytoplasm, disulfide bonds between cysteine residues help to maintain the tertiary structure.

When the local pH drops, the protein undergoes an energetically favorable conformational rearrangement that enables it to penetrate the host cell membrane.

Protein chaperones within the cytoplasm of a cell assist a newly synthesised polypeptide to attain its native state.

[8] Structure stabilized by the formation of weak bonds between amino acid side chains - Determined by the folding of the polypeptide chain on itself (nonpolar residues are located inside the protein, while polar residues are mainly located outside) - Envelopment of the protein brings the protein closer and relates a-to located in distant regions of the sequence - Acquisition of the tertiary structure leads to the formation of pockets and sites suitable for the recognition and the binding of specific molecules (biospecificity).

It provides high resolution of the structure but it does not give information about protein's conformational flexibility.

Cryogenic electron microscopy (cryo-EM) can give information about both a protein's tertiary and quaternary structure.

Dual polarisation interferometry provides complementary information about surface captured proteins.

[11][12] Protein structure prediction is a new way to create disease models, which may avoid the use of animals.

The CoMOGrad project at BUET is a research effort to device an extremely fast and much precise method for protein tertiary structure retrieval and develop online tool based on research outcome.