(Solomon, Martin, Martin, & Berg, 2015) Its atom makes up is carbon (C), hydrogen (H), oxygen (O), nitrogen (N) and small amounts of sulfate (S). There are 20 different amino acids used in the make up proteins. There build up includes an amino group, a carboxyl functional group, and a designated R-group. However, the differences they contain stand within there R-groups which are used in the identification of each amino acid. There R-groups help determines if the protein is polar, non-polar, hydrophobic and/or hydrophilic. Proteins have four structure called primary, secondary, tertiary and quaternary. Primary structures are an amino acid sequence determined DNA. This is what helps peptide bonds, which are two amino acids connected by the N-containing base and carboxyl group hold together. Secondary structures are interactions between the “NH2” and the “COOH” of non-adjacent amino acids. Hydrogen bonds which are bonds between a hydrogen of a polar molecule plus a accuracy negative atom of another molecule hold this structure together. Tertiary structures are the “R-group” that start to interact resulting in the proteins to fold into a 3D form. Hydrogen, covalent which are atoms that share electrons between two atoms and ionic which are forms between two charged atoms bonds can be formed from this structure. If the amino acid is hydrophobic it will fold inward and if the amino acid is hydrophilic it will fold outward. Quaternary Structures are two or more polypeptides bound together to form a complex protein. Hydrogen, covalent and ionic bonds can also be formed from this structure. Proteins can become denatured meaning that when the bond that holds tertiary structures together breaks due to it being heated or having a change in
(Solomon, Martin, Martin, & Berg, 2015) Its atom makes up is carbon (C), hydrogen (H), oxygen (O), nitrogen (N) and small amounts of sulfate (S). There are 20 different amino acids used in the make up proteins. There build up includes an amino group, a carboxyl functional group, and a designated R-group. However, the differences they contain stand within there R-groups which are used in the identification of each amino acid. There R-groups help determines if the protein is polar, non-polar, hydrophobic and/or hydrophilic. Proteins have four structure called primary, secondary, tertiary and quaternary. Primary structures are an amino acid sequence determined DNA. This is what helps peptide bonds, which are two amino acids connected by the N-containing base and carboxyl group hold together. Secondary structures are interactions between the “NH2” and the “COOH” of non-adjacent amino acids. Hydrogen bonds which are bonds between a hydrogen of a polar molecule plus a accuracy negative atom of another molecule hold this structure together. Tertiary structures are the “R-group” that start to interact resulting in the proteins to fold into a 3D form. Hydrogen, covalent which are atoms that share electrons between two atoms and ionic which are forms between two charged atoms bonds can be formed from this structure. If the amino acid is hydrophobic it will fold inward and if the amino acid is hydrophilic it will fold outward. Quaternary Structures are two or more polypeptides bound together to form a complex protein. Hydrogen, covalent and ionic bonds can also be formed from this structure. Proteins can become denatured meaning that when the bond that holds tertiary structures together breaks due to it being heated or having a change in