Tehdyt toimenpiteet

Protein research

All proteins consist of a chain made up of twenty different amino acids. The length of the chain ranges from a couple dozen to thousands of amino acids. DNA determines the place for each amino acid in the protein molecule chain.

These amino acid chains fold into a structure characteristic of each protein family. The structures may consist of spirals, pleats, sheets or other three-dimensional shapes. In natural conditions, the folding of an amino acid chain lasts from microseconds to several seconds, depending on the protein. During the folding, the protein goes through thousands of different shapes before it reaches its functional conformation. An error in folding may cause a disease.

To fold correctly, a protein sometimes needs interaction with other proteins. Other factors also affect the folding, such as the temperature, mutations of the amino acid chain, or the concentrations of other molecules, e.g., salts. The information needed for the correct folding of a protein is contained in the protein’s amino acid sequence. Folding is a complex event that can be studied with the help of computers. Modeling the folding of a protein by means of simulations requires huge computer capacity.

The three-dimensional structure of proteins has a greater impact on their function than the amino acid sequence. Even if their amino acid sequences differ by as much as 90 per cent, proteins of a similar shape can functionally resemble each other very much. The three-dimensional structures determined for proteins have been collected into a database that is open to the scientific community.

Not as many new protein folds are found today as in the past. It has therefore been concluded that there is a maximum number of protein folds existing among living organisms. When the structure of one member of a protein family (a group of proteins with a similar structure) is known, an attempt can be made to create a model of the structure of the other members. The Human Genome Project has made it possible to determine the amino acid sequences of human proteins, and the three-dimensional structures of proteins can be solved by studying their folding.

The structure of a protein opens up a way for understanding, and even controlling, its function. Proteins can be controlled with medications: small molecules that block or accelerate the function of a protein. Better understanding of the folding and interactions of proteins is therefore one key in our efforts to develop better medicines in the future.

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Tehdyt toimenpiteet

Protein research


Sisältö Methods of computational science Applications of scientific computing Modeling the universe Ships and computational fluid dynamics Protein research Drug design Speech recognition and synthetic speech Modeling the human body Modeling in geosciences Geographic information systems Genotype and bioinformatics Grand Challenge research projects in CSC magazines Supercomputers and grids	Tehdyt toimenpiteet Tämä sivu suomeksi Protein research All proteins consist of a chain made up of twenty different amino acids. The length of the chain ranges from a couple dozen to thousands of amino acids. DNA determines the place for each amino acid in the protein molecule chain. These amino acid chains fold into a structure characteristic of each protein family. The structures may consist of spirals, pleats, sheets or other three-dimensional shapes. In natural conditions, the folding of an amino acid chain lasts from microseconds to several seconds, depending on the protein. During the folding, the protein goes through thousands of different shapes before it reaches its functional conformation. An error in folding may cause a disease. To fold correctly, a protein sometimes needs interaction with other proteins. Other factors also affect the folding, such as the temperature, mutations of the amino acid chain, or the concentrations of other molecules, e.g., salts. The information needed for the correct folding of a protein is contained in the protein’s amino acid sequence. Folding is a complex event that can be studied with the help of computers. Modeling the folding of a protein by means of simulations requires huge computer capacity. The three-dimensional structure of proteins has a greater impact on their function than the amino acid sequence. Even if their amino acid sequences differ by as much as 90 per cent, proteins of a similar shape can functionally resemble each other very much. The three-dimensional structures determined for proteins have been collected into a database that is open to the scientific community. Not as many new protein folds are found today as in the past. It has therefore been concluded that there is a maximum number of protein folds existing among living organisms. When the structure of one member of a protein family (a group of proteins with a similar structure) is known, an attempt can be made to create a model of the structure of the other members. The Human Genome Project has made it possible to determine the amino acid sequences of human proteins, and the three-dimensional structures of proteins can be solved by studying their folding. The structure of a protein opens up a way for understanding, and even controlling, its function. Proteins can be controlled with medications: small molecules that block or accelerate the function of a protein. Better understanding of the folding and interactions of proteins is therefore one key in our efforts to develop better medicines in the future.