Hydrogen bonds are important for the formation of hydride bridges. These cause the protein molacules to twist into their unusual shapes. Many proteins are used in "lock and key" processes throughout the cells. Without the proper shape, the keys will no longer fit and the protein is useless for continuing the process.
Protein structure is partially determined by hydrogen bonding. Hydrogen bonds can occur between a hydrogen on an amine and an electronegative element, such as oxygen on another residue. As a protein folds into place, a series of hydrogen bond "zips" the molecule together, holding it in a specific three-dimensional form that gives the protein its particular function.
Protein folding determines the shape of the protein, and thus what it does, because it is the shape of the protein which enables it to perform its function. For example, enzymes need to have exactly the right shape to fit with the molecules they are working with to catalyze them. Also, hemoglobin is specifically folded with four pocket like areas to allow oxygen to attach to it. The shape of the protein is specific to the function that it is performing, and is different for each protein. If there is even a slight change in the make up of the protein, or a mutation (the amino acids are messed up) then the protein will fold differently. Even a slight change in the composition of the protein can disable the protein from properly performing the function which it is meant to do.
Well, in the case of DNA (which is, next to RNA, one of the most important nucleic acids), hydrogen bonds are present between complementary base pairs: Guanine hydrogen bonds to cytosine, and adenine hydrogen bonds to thymine (or uracil, in the case of certain RNA strands). These hydrogen bonds therefore greatly influence the 3-dimensional structure of DNA (i.e. its helical structure).
Protein folding determines the shape of the protein, and thus what it does, because it is the shape of the protein which enables it to perform its function. For example, enzymes need to have exactly the right shape to fit with the molecules they are working with to catalyze them. Also, hemoglobin is specifically folded with four pocket like areas to allow oxygen to attach to it. The shape of the protein is specific to the function that it is performing, and is different for each protein. If there is even a slight change in the make up of the protein, or a mutation (the amino acids are messed up) then the protein will fold differently. Even a slight change in the composition of the protein can disable the protein from properly performing the function which it is meant to do.
Hydrogen bonds hold the nitrogenous bases together in DNA. The nitrogenous bases are adenine,thymine,guanine,cytosine, or uracil.
hydrogen bonds
A water molecule is formed when two hydrogen atoms bind covalently to a single oxygen atom.
Hydrogen bonds with hydrogen bond acceptor atoms such as Oxygen. Covalent bonds with nearly anything.
There are a few types of hydrogen bonds. Fluorine, oxygen, and nitrogen are the elements that typically form bonds with hydrogen.
Hydrogen bonds are not the weakest bonds.
Hydrogen bonds are considered weak bonds, however in large biochemical molecules, they can act as a stabilizer. An example is a protein, which contains numerous weak bonds (Hydrogen, van der Waals, and hydrophobic), after the primary structure.
A hydrogen acceptors for hydrogen bonds is nitrogen.
Hydrogen bonds
It is the hydrogen wich bonds between AT and GC the difference is in the number AT have 2 hydrogen bonds GC have 3 hydrogen bonds
hydrogen bonds
There are no hydrogen bonds in HF.
It is not covalent, because it is the strongest type. The Correct answer is van der Waals.
yes it can when it dissolves in water in forms hydrogen bonds in fact its the one that has the most hydrogen bonds
hydrogen bonds hold DNA together
Strong hydrogen bonds.
Hydrogen bonds are betweem molecules and are weak forces.
Silicon has 4 bonds with hydrogen