Profile
Detailed Description of the Institute
Proteins are the workbench of life processes. They contribute to metabolic reactions, the transformation of energy forms, defense against illness, and many other life phenomena - with a high degree of efficiency and precision. To meet the various tasks, proteins have only a very limited number of basic building materials at their disposal, which nature characteristically binds together by the hundreds for each individual function. In a manner that is not yet understood, the resulting protein chains fold to create characteristically formed molecules. These molecules often work by the dozen to react to environmental stimuli or to allow a lifecycle to elapse. The smooth functioning of life processes depends on the correct three-dimensional structure of protein chains.
We are investigating to what extent proteins assist each other when forming correct, functional structures and whether intermediate states during folding provide a necessary contribution to the smooth functioning of cellular processes. Chaperones and prolyl isomerases belong to the class of folding helper proteins, which are produced during the intermediate states of unfolded or partially folded protein chains. Researchers use physical measuring techniques to determine the structure of proteins in their active form within the cell. Measurement results indicate, that to fulfill their biological function, the internal movements of proteins must take place within a definite timeframe.
This motion is quite typical in the proximity of proline, a kind of amino acid. Protein molecules acting as biocatalysators have been identified in nearly all biological material studied to date. They increase the mobility of protein chains in the presence of proline. Only three large families of biocatalysators have been identified to date that occur as cells, tissues, and bodily fluids in dozens of variously constructed single proteins. They occur in humans as well as primitive forms of bacteria. The identification and decoding of the structures of biocatalysators is a basic precondition for further research into assisted folding reactions. However, this alone cannot provide information on their role in life processes. Work in this area will require the help of molecular biology, cell biology, and chemical synthesis.
The role of these biocatalysators has been established in a variety of processes, including the spread of infectious disease, the control of cell division and signal transduction, the synthesis of connective tissue, and in sight processes. Such discoveries are anticipated from our facilities in the future. Detection methods are an essential factor in the search for biocatalysators. They must be sufficiently sensitive and applicable. The search for potential medicines based on effectors for folding helper catalysators should be simplified by the development of an automated system suitable for "high-throughput" methodology.
Proteins are the workbench of life processes. They contribute to metabolic reactions, the transformation of energy forms, defense against illness, and many other life phenomena - with a high degree of efficiency and precision. To meet the various tasks, proteins have only a very limited number of basic building materials at their disposal, which nature characteristically binds together by the hundreds for each individual function. In a manner that is not yet understood, the resulting protein chains fold to create characteristically formed molecules. These molecules often work by the dozen to react to environmental stimuli or to allow a lifecycle to elapse. The smooth functioning of life processes depends on the correct three-dimensional structure of protein chains.
We are investigating to what extent proteins assist each other when forming correct, functional structures and whether intermediate states during folding provide a necessary contribution to the smooth functioning of cellular processes. Chaperones and prolyl isomerases belong to the class of folding helper proteins, which are produced during the intermediate states of unfolded or partially folded protein chains. Researchers use physical measuring techniques to determine the structure of proteins in their active form within the cell. Measurement results indicate, that to fulfill their biological function, the internal movements of proteins must take place within a definite timeframe.
This motion is quite typical in the proximity of proline, a kind of amino acid. Protein molecules acting as biocatalysators have been identified in nearly all biological material studied to date. They increase the mobility of protein chains in the presence of proline. Only three large families of biocatalysators have been identified to date that occur as cells, tissues, and bodily fluids in dozens of variously constructed single proteins. They occur in humans as well as primitive forms of bacteria. The identification and decoding of the structures of biocatalysators is a basic precondition for further research into assisted folding reactions. However, this alone cannot provide information on their role in life processes. Work in this area will require the help of molecular biology, cell biology, and chemical synthesis.
The role of these biocatalysators has been established in a variety of processes, including the spread of infectious disease, the control of cell division and signal transduction, the synthesis of connective tissue, and in sight processes. Such discoveries are anticipated from our facilities in the future. Detection methods are an essential factor in the search for biocatalysators. They must be sufficiently sensitive and applicable. The search for potential medicines based on effectors for folding helper catalysators should be simplified by the development of an automated system suitable for "high-throughput" methodology.