secondary structure
The main difference between a right-handed alpha helix and a left-handed alpha helix in protein structures is the direction in which the helix twists. In a right-handed alpha helix, the helix twists in a clockwise direction, while in a left-handed alpha helix, the helix twists in a counterclockwise direction. This difference in twisting direction affects the overall shape and stability of the protein structure.
The coiling of the protein chain backbone into an alpha helix represents the secondary structure of a protein. This structure is stabilized by hydrogen bonds between the amino acid residues in the protein chain, forming a corkscrew-like structure.
The coiling of the protein chain backbone into an alpha helix is referred to as secondary structure. This repetitive structure is stabilized by hydrogen bonds between the backbone amide hydrogen and carbonyl oxygen atoms.
He is famous because of his research of Alpha Helix protein structure. It is spiral chain of amino acids stabilized by hydrogen bonds.http://www.answers.com/topic/alpha-helix
He is famous because of his research of Alpha Helix protein structure. It is spiral chain of amino acids stabilized by hydrogen bonds.http://www.answers.com/topic/alpha-helix
The alpha helix protein helps form the structure of the cell membrane by creating channels and pores that allow substances to pass through. It also helps maintain the integrity and stability of the membrane.
A collagen helix is less compact (because it goes into triple helices), and it is a left-handed helix. An alpha helix is more compact and hence requires more rotation of bonds to form (hence proline is not very common...has an imidazole ring). It is a right-handed helix, and goes into double helices instead.
together they make a secondary protein structure
The alpha helix and beta pleated sheet represent the secondary structure of proteins. Both structures are formed by the interaction of amino acids within the polypeptide chain through hydrogen bonding.
The spiral shape of a coiled protein is called an alpha helix. This secondary structure is formed by hydrogen bonds between amino acids in the protein chain, resulting in a tightly wound helical structure.
Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape
The process of a protein unfolding is called denaturation. During denaturation normal alpha-helix and beta sheets are disrupted causing the protein to uncoil and become misshaped