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Primary- Covalent bonds Secondary- Hydrogen bonds Tertiary- Hydrophobic interactions - Disulphide bonds/bridges - Hydrogen bonding Quaternary- (Same as Tertiary)
tetrahedron
Proteins are composed of amino acids, each of which have their own special properties. The nonpolar amino acids would fold into the interior of the protein during protein folding, because they are hydrophobic. A protein consists of a primary structure, which consists of the amino acid chain. The secondary structure is how the amino acids join together into alpha helixes and beta pleated chains and form hydrogen bonds. The tertiary structure is when disulfide bridges form, which maintain the protein's 3-d shape, and the 3-d shape begins to emerge. The quarternary structure is an assortment of several polypeptides, and constitutes the entire protein. The final shape of the protein determines its function.
Carbon (C) has four valence electrons (electrons in the outer shell) and it needs 4 more to fulfill the octet (8) rule. Therefore carbons will make four bonds. The structure H-C=C-H is nonsensical because the carbons only have 3 bonds each.
Carbon usually forms four single bonds in its compounds. Of course, if multiple bonds are present, then the number is different. In the case of multiple bonds, carbon forms two double bonds or a triple bond and one single bond.
Primary- Covalent bonds Secondary- Hydrogen bonds Tertiary- Hydrophobic interactions - Disulphide bonds/bridges - Hydrogen bonding Quaternary- (Same as Tertiary)
the primary structure is the lowest level
There are four distinct levels of protein structure. The main two are primary, amino acid, secondary structure, and quaternary structure.
There are four types of protein structure. These include primary structure, secondary structure, tertiary structure, and quaternary structure. Primary structure is the amino acid sequence. Secondary structure is the shape of the molecule. Tertiary structure is the interaction between groups. Quaternary structure is the interactions between protein subunits.
tetrahedron
Quaternary
Carbon will form four covalent bonds, nitrogen will form three covalent bonds, oxygen will form two covalent bonds, and hydrogen will form one covalent bond. Click on the related link to see a diagram showing the structure of an amino acid.
Carbon has 4 valence electrons, allowing it to form 4 covalent bonds to achieve a full outer shell, which is more stable. By sharing electrons with other atoms, carbon can achieve a total of 8 electrons in its outer shell, following the octet rule.
The four levels of protein structure are differentiated from each other by the complexity of their polypeptide chain. Proteins are constructed from 20 amino acids. The levels are the hydrogen atom, a Carboxyl group, an amino group and a variable or "R" group. They have a primary structure, the order in which the amino acids are linked to form a protein. Secondary structure , coiling and folding of the polypeptide chain. Tertiary structure, is a 3-D structure of a protein chain. Quaternary is the structure of a protein macro molecule formed by interactions between several polypeptide chains..
The smaller building blocks of protein are called amino acids. Amino acids are molecules containing a carboxyl group (-COOH), an amino group (-NH2) and a variable or "R" group, which is what makes the different types of amino acids. There are 20 different amino acids, but they can be arranged into many different sequences, which explains why so many different proteins exist. Amino acids form long chains called polypeptide chains. These chains can then fold into a secondary structure, either an alpha helix or a beta pleated sheet. Then that continues to be folded into the tertiary structure, which is formed by four different types of bonds: hydrogen bonds, hydrophobic interactions, ionic bonding and disulfide bridges. Tertiary folding can have two shapes, coils or barrels. Finally there is quaternary structure, which contains multiple polypeptide chains folded into rounded shapes. Quaternary structure has two different shapes, fibrous and globular.
Carbon has four valence electrons, each of which can be shared to form four single bonds. This means that it is possible to have two double bonds.
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.