Answer:
A. Only L-amino acids (except for glycine) are used in proteins.
B. The partial double bond character of the α-C-N bond in the peptide group limits the conformations of the peptide group.
C. Hydrogen bonding within elements of secondary structure stabilize certain atomic geometries.
D. Although any one of 20 amino acids is possible at each position, only one is used.
Explanation:
Proteins are biomolecules composed of one or more chains of amino acid residues which are joined together by peptide bonds (this sequence represents the primary structure of the protein). Proteins are made up of 20 types of amino acids which have diverse properties. The secondary structure of a protein refers to the local structure of the protein backbone, which is stabilized by hydrogen bonding between amino groups (—NH2) and carboxyl groups (—COOH) in neighboring areas of the protein. The most common secondary structures in proteins include alpha helices, beta sheets, and random turns. Moreover, the tertiary structure in proteins describes the packing of these secondary structures. The peptide bond (CO–NH) is a stable covalent bond that has a rigid planar structure and acquires partial double-bond properties, thereby peptide bonds undergo very little rotation (i.e., rotation around peptide bonds is restricted). With the exception of glycine, all amino acids are stereoisomers, i.e., there exist mirror images of their structures which are labeled as L (left-handed) and D (right-handed) in order to differentiate between mirror images. All amino acids in proteins have the L-configuration.
Answer:
The speed of a reaction is given by the reaction rate, a measure of how fast reactants are consumed and products are formed. The study of reaction rates is known as chemical kinetics. The central theory of kinetics is collision theory. The premise of this theory is simple: molecules have to collide to react.
Explanation:
Lionization is the answers me
Because it doesnt have cell wall nor chloroplast
Answer:
Enterokinase is produced by the duodenal mucosa. It activates trypsin, a pancreatic proteolytic enzyme, which in turn activates the remainder of the enzymes facilitating protein digestion. The pancreas releases other proteolytic enzymes into the intestine that continue the digestive process.
Explanation:
