Importance of Hydrogen Bonding in Maintaining Protein Structure

The construction of large structures, ensure that the structure is solid, clean and ready to review your goals. In very large structures in the case of buildings, builders build more than one column to the floor and a triangle, like logs in the ceiling, they do not interfere, do not have construction, "and to prevent the building of the destruction. After a column in the center of the conference room was not appropriate, then, when these support units will be installed must be considered. That is the structure of the proteins that form the links at certain points in certain quantities, protein strong enough to handle due to their work. These bonds are called hydrogen bonds.
Hydrogen bonds are non-covalent means to create an electrostatic attraction between the atoms of positively and negatively charged and are formed spontaneously without enzymatic catalysis (1). However, they are quite low, so little energy is needed to break these links. This can be an advantage, as well as a lack, however, and structures that are not connected by hydrogen bonds are very strong, they are flexible enough that can be useful if the structure has to change its shape according to their function. That's where the squirrels come to play.
Protein is found everywhere, and between cells, so many jobs. They have a special 3-D that relate directly to function, so there are a variety of proteins, but each has different tasks and do not interfere with each other.
Hydrogen bonds in protein structure
The proteins are synthesized in the cytoplasm of the cell, if the core of the mRNA codon is associated with the tRNA anti-codon in the synthesis of amino acids, proteins, base stations results. Proteins have four levels of the organization with the name of the primary, secondary structure, tertiary and quaternary (2). The primary structure refers to the amino acid sequence, secondary structure formed by the alpha helix and beta-sheet tertiary structure of polypeptide chains and folded quaternary structure of the association of the subunits of the protein in most . Hydrogen bonds involved in secondary structure, tertiary and quaternary structure of proteins. As the amino acids in proteins behave?
After a sequence of amino acids determines the alpha helix is ​​formed, the formation of hydrogen bonds between the CO and NH = groups of amino acids. Then the beta-sheet is formed with the formation of hydrogen bonds between polypeptide chains. Proteins have a stable structure, forming a hydrogen bond in the right places. Then, the polypeptide chains begin depending on where the hydrogen bonds are formed when secondary structure, hydrogen bonding also plays an important role in the shape of the protein to maintain its tertiary structure. Then fold the polypeptide chain, they need help to get fit and make hydrogen bonds are available to all other obligations of this period, including covalent bonds and disulfide bonds (3). Finally, the quaternary structure exists only in the proteins that contain more than one polypeptide. Hydrogen bonds are also found in the quaternary structure.
Completion
As we can see the hydrogen bonds play an important role in maintaining the shape of the protein. According to the primary structure, are formed in some places and to determine all other levels of the organization of proteins. Without them, the tertiary structure of proteins that bind a different value and can not interact with molecules it needs cause it to malfunction, which are proteins. Hydrogen bonds are compared the positions set, you can break easily, but if you get ten of them together they become stronger and more, and not the function of proteins that Alive!