Kunavina Kristina Biotechnology презентация

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Folding. What is it?

In biochemistry and molecular biology, protein folding is

Folding. What is it? In biochemistry and molecular biology, protein folding is the
the process of spontaneous folding of a polypeptide chain into a unique native spatial structure.
Each protein molecule begins to form as a polypeptide translated from the mRNA sequence in the form of a linear chain of amino acids. The polypeptide does not have a stable three-dimensional structure (example on the left side of the image).

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Chaperones

To ensure folding, a group of auxiliary proteins called chaperones is

Chaperones To ensure folding, a group of auxiliary proteins called chaperones is used.
used. They prevent the interaction of newly synthesized proteins with each other, isolate the hydrophobic portions of proteins from the cytoplasm and "remove" them inside the molecule, the protein domains are correctly positioned.

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Fundamental problems of folding

The problem is that humanity, with all its

Fundamental problems of folding The problem is that humanity, with all its computing
computing power and an arsenal of experimental data, still has not learned how to build models that describe the process of protein folding and predict the three-dimensional structure of a protein based on its primary structure (i.e. amino acid sequence). Thus, there is still no full understanding of this physical process.

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What is being done to solve the problem?

There are two groups

What is being done to solve the problem? There are two groups of
of structure prediction methods:
The first includes the so-called modeling methods “from scratch”
The second group of methods includes comparative modeling methods.

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Coagulation mechanisms of protein molecules

Coagulation of the polypeptide chain into the

Coagulation mechanisms of protein molecules Coagulation of the polypeptide chain into the native
native conformation is most successful under physiological conditions. The loss of native conformation, denaturation, occurs at extreme pH, high temperature or under the influence of organic solvents, detergents and other denaturing substances.

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Examples

Consider a few examples, globular proteins built from α-helices, such as

Examples Consider a few examples, globular proteins built from α-helices, such as myoglobin,
myoglobin, are rare. Usually there are combinations of folded sheets and spiral sections, such as, for example, in flavodoxin, a small flavoprotein, where 5 fan-folded sheets of five parallel strands form the nucleus of the molecule; 4 α-helical regions surround the core from the outside. Immunoglobulin is constructed from several similar domains (independent, compactly folded fragments of the polypeptide chain) in which two antiparallel folded sheets of three or four strands form a barrel-shaped structure.The oligonucleotide shown in the diagram shows the CH2 domain.
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