leu gly pro secondary structure primary str (a-helix) (amino acid s
tertiary structure (folded individual peptide)
quaternary structure (aggregation of two or more peptides
The secondary structure is the tendency of the polypeptide to coil or pleat due to H-bonding between R-groups. The tertiary structure is controlled by bonding(or in some cases repulsion) between r groups. Many proteins, such as hemoglobin, are formed from one or more polypeptides. Such structure is termed quaternary structure Structural proteins, such as collagen, have regular repeated primary structures. Like the structural carbohydrates, the components determine the final shape and ultimately function. Collagens have a variety of functions in living things, such as the tendons, hide, and corneas of a cow. Keratin is another structural protein. It is found in fingernails, feathers hair, and rhinoceros horns microtubules important in cell division and structures of flagella and cilia (among other things), are composed of globular structural proteins
The secondary structure is the tendency of the polypeptide to coil or pleat due to H-bonding between R-groups. The tertiary structure is controlled by bonding (or in some cases repulsion) between Rgroups. Many proteins, such as hemoglobin, are formed from one or more polypeptides. Such structure is termed quaternary structure. Structural proteins, such as collagen, have regular repeated primary structures. Like the structural carbohydrates, the components determine the final shape and ultimately function. Collagens have a variety of functions in living things, such as the tendons, hide, and corneas of a cow. Keratin is another structural protein. It is found in fingernails, feathers, hair, and rhinoceros horns. Microtubules, important in cell division and structures of flagella and cilia (among other things), are composed of globular structural proteins
B ase Base (pyrimidine)(purine) Sugar- (a)Nucleotide phosphate (b)Nucleotide