By Denise R. Ferrier
Lippincott’s Illustrated stories: Biochemistry is the normal first-and most sensible source for the necessities of biochemistry. scholars depend on this article to assist them speedy review, assimilate, and integrate quite a lot of serious and intricate info. For greater than twenty years, school and scholars have praised LIR Biochemistry’s matchless illustrations that make strategies come to life.NEW! • huge revisions and up to date content
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Extra info for Biochemistry (Lippincott's Illustrated Reviews Series)
For example, a tripeptide composed of an N-terminal valine, a glycine, and a C-terminal leucine is called valylglycylleucine. 2. 2B). This prevents free rotation around the bond between the carbonyl carbon and the nitrogen of the peptide bond. However, the bonds between the α-carbons and the α-amino or α-carboxyl groups can be freely rotated (although they are limited by the size and character of the R groups). This allows the polypeptide chain to assume a variety of possible configurations. 2B), in large part because of steric interference of the R groups when in the cis position.
However, others may consist of two or more polypeptide chains that may be structurally identical or totally unrelated. The arrangement of these polypeptide subunits is called the quaternary structure of the protein. Subunits are held together primarily by noncovalent interactions (for example, hydrogen bonds, ionic bonds, and hydrophobic interactions). Subunits may either function independently of each other or may work cooperatively, as in hemoglobin, in which the binding of oxygen to one subunit of the tetramer increases the affinity of the other subunits for oxygen (see p.
Helix Several different polypeptide helices are found in nature, but the α helix is the most common. 6). A very diverse group of proteins contains α-helices. For example, the keratins are a family of closely related, fibrous proteins whose structure is nearly entirely α-helical. They are a major component of tissues such as hair and skin, and their rigidity is determined by the number of disulfide bonds between the constituent polypeptide chains. In contrast to keratin, myoglobin, whose structure is also highly α-helical, is a globular, flexible molecule (see p.