Proteins serve all of these functions and many more. Most enzymes are proteins, which help to catalyze spontaneous reactions. Ribozymes can also serve this function but are instead made out of RNA. Proteins can act as transcriptional regulators which can turn on or off gene transcription. Structural proteins, such as actin, can help to maintain the shape of a cell. Other small proteins, such as insulin, can act as hormones which can diffuse throughout the body relaying important messages.

Proteins serve all of these functions and many more. Most enzymes are proteins, which help to catalyze spontaneous reactions. Ribozymes can also serve this function but are instead made out of RNA. Proteins can act as transcriptional regulators which can turn on or off gene transcription. Structural proteins, such as actin, can help to maintain the shape of a cell. Other small proteins, such as insulin, can act as hormones which can diffuse throughout the body relaying important messages.

Proteins serve all of these functions and many more. Most enzymes are proteins, which help to catalyze spontaneous reactions. Ribozymes can also serve this function but are instead made out of RNA. Proteins can act as transcriptional regulators which can turn on or off gene transcription. Structural proteins, such as actin, can help to maintain the shape of a cell. Other small proteins, such as insulin, can act as hormones which can diffuse throughout the body relaying important messages.

Fatty acids synthesized in the human body always have an even number of carbon atoms usually between 12 and 28. Odd-numbered fatty acid chains will occasionally be found in plants and marine animals.

Fatty acids synthesized in the human body always have an even number of carbon atoms usually between 12 and 28. Odd-numbered fatty acid chains will occasionally be found in plants and marine animals.

Fatty acids synthesized in the human body always have an even number of carbon atoms usually between 12 and 28. Odd-numbered fatty acid chains will occasionally be found in plants and marine animals.

Ionic bonds, disulfide bridges, hydrogen bonds and hydrophobic interactions are all examples of protein tertiary structure when they occur within a single polypeptide chain. However, if these interactions were to occur between separate polypeptide chains then they would be defining the quaternary structure of the protein. The linear sequence of amino acids within a protein makes up the primary structure. Protein secondary structure is defined by the localized three-dimensional structure of amino acids. These localized structures are normally constructed through hydrogen bonding networks. Alpha helices and Beta pleated sheets are examples of secondary structures.

Ionic bonds, disulfide bridges, hydrogen bonds and hydrophobic interactions are all examples of protein tertiary structure when they occur within a single polypeptide chain. However, if these interactions were to occur between separate polypeptide chains then they would be defining the quaternary structure of the protein. The linear sequence of amino acids within a protein makes up the primary structure. Protein secondary structure is defined by the localized three-dimensional structure of amino acids. These localized structures are normally constructed through hydrogen bonding networks. Alpha helices and Beta pleated sheets are examples of secondary structures.

Ionic bonds, disulfide bridges, hydrogen bonds and hydrophobic interactions are all examples of protein tertiary structure when they occur within a single polypeptide chain. However, if these interactions were to occur between separate polypeptide chains then they would be defining the quaternary structure of the protein. The linear sequence of amino acids within a protein makes up the primary structure. Protein secondary structure is defined by the localized three-dimensional structure of amino acids. These localized structures are normally constructed through hydrogen bonding networks. Alpha helices and Beta pleated sheets are examples of secondary structures.

Enzymes are used to increase the rate of a reaction. This is accomplished by lowering the activation energy required for substrates to react, often by altering the transition state. Enzymes do not, however, increase the amount of products formed; they simply help the equilibrium be reached more quickly. In other words, enzymes change the rate of a reaction, but not the equilibrium.