For instance, to determine the secondary structures of the protein, it is necessary to analyze the hydrogen bonding patterns and geometric constraints, and to use the DSSP tool. To determine the protein structures, laboratory methods are applied, such as X-ray crystallography, multidimensional nuclear magnetic resonance, and infrared spectroscopy, with a complex interpretation of the results. The most common method in the literature is to first understand the secondary structure and then predict the tertiary structure. Recent work has shown that the prediction of the tertiary structure, directly from the primary structure, can achieve good results, but this task is still open. Īnalyzing the three-dimensional structures of proteins has a great impact on determining the protein functions, mainly because each function depends on a specific folding, and each protein can exert more than one function, as well as the development of new applications, such as drug and enzyme design and biosensors. The local three-dimensional structure that each amino acid participates in is called the secondary structure, whereas three-dimensional structure that the protein forms is called the tertiary structure. Amino acids interact physically and chemically with each other, forming three-dimensional structures.
They are formed by a sequence of amino acids, which consist of the protein’s primary structure. Proteins are present in many biological processes in the cells of living beings, playing different functions, such as transport, growth, and maintenance of the body.
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