B DNA has a wide and deep major groove and a narrow and deep minor groove. All other statements regarding B DNA are true.

In DNA and RNA, there are two types of nitrogenous bases: pyrimidines and purines. A pyrimidine contains one carbon-nitrogen ring with two nitrogen atoms. A purine consists of a pyrimidine fused with an imidazole ring. Adenine and guanine are purines. Cytosine, thymine, and uracil are pyrimidines.

Trypsin will cleave the primary sequence after the lysine residue (on its carboxyl side). Thus, Lys will be the new carboxyl terminal and Glu will be the new amino terminal. Remember that a protein's primary sequence is written from N to C.

When a protein is damaged, it can be tagged with the molecule, ubiquitin. This signals to the cell that the protein is no longer functioning properly and needs to be degraded.

The backbone of DNA is made up of alternating phosphate groups and sugar groups, linked together via phosphodiester bonds. The nitrogenous bases jut off of the backbone and form bonds with nitrogenous bases on other strands of DNA to become double stranded. A nucleotide consists of a sugar, nitrogenous base, and one or more phosphate groups.

In DNA and RNA, there are two types of nitrogenous bases: pyrimidines and purines. A pyrimidine contains one carbon-nitrogen ring with two nitrogen atoms. A purine consists of a pyrimidine fused with an imidazole ring. Adenine and guanine are purines. Cytosine, thymine, and uracil are pyrimidines.

Trypsin will cleave the primary sequence after the lysine residue (on its carboxyl side). Thus, Lys will be the new carboxyl terminal and Glu will be the new amino terminal. Remember that a protein's primary sequence is written from N to C.

A peptide bond connects two amino acids. This is the result of a condensation reaction (water is lost) and a new nitrogen-carbon bond forms between two amino acids. Note that amino acid synthesis occurs in the direction. Peptide bonds are covalent bonds that are responsible for the primary structure of amino acids.

An O-linked glycoprotein is a protein that has a sugar attached to it. It is called O-linked because the sugar is attached to an oxygen atom on either a threonine residue or a serine residue within the protein.

In a globular protein, the amino acid chain can twist in a way that polar groups lie at the protein's surface. This allows the protein to interact with water and enhances the protein's solubility in water. This does not occur in fibrous proteins, so fibrous proteins are insoluble in water.