yes
Yes, they do. Side group hydrogen bonding.
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.
Hemoglobin does not contain beta sheets. It is a globular protein composed of four subunits - two alpha and two beta subunits in adults (hemoglobin A). Each subunit consists of alpha-helices, not beta sheets.
Amylase helps the body digesting starch. Different types of amylase (alpha, beta...) can split different types of starch into sugar units.
The optimum pH is neutral, 7.
together they make a secondary protein structure
Ptyalin is an alpha-amylase. It is the alpha-amylase found in saliva
Hydrogen bonding is the primary interaction that stabilizes the alpha helix and beta pleated sheets of a protein. In the case of alpha helices, hydrogen bonds form between the carbonyl oxygen of one amino acid residue and the amide hydrogen of another residue in the chain. In beta sheets, hydrogen bonds form between adjacent strands of the sheet.
The secondary structures of alpha helix and beta pleated sheets are formed by hydrogen bonding between amino acids in a protein chain. In an alpha helix, the hydrogen bonding occurs between amino acids in the same chain, leading to a helical structure. In beta pleated sheets, hydrogen bonding occurs between amino acids in different segments of the protein chain, creating a sheet-like structure.
protein secondary structures, which are common motifs found in protein folding. Alpha helices are formed by a right-handed coil of amino acids stabilized by hydrogen bonding, while beta-pleated sheets are formed by hydrogen bonding between adjacent strands of amino acids running in parallel or antiparallel orientation.
The two types of tertiary protein structures: globular and fibrous proteins. Globular proteins act as enzymes that catalyze chemical reactions in organisms. Fibrous proteins like collagen play structural role.
Yes, they do. Side group hydrogen bonding.
Alpha bonds are hydrolised by alpha amylase. The alpha amylase is the sole form of amylase found in all mammals.
Amylase is an enzyme that induces hydrolysis of starches, breaking them down into sugar. Saliva alpha amylase is simply a type of amylase.
Alpha amylase and beta amylase are enzymes that break down starch, but they have different functions. Alpha amylase breaks down starch into maltose and other sugars, while beta amylase specifically breaks down starch into maltose. Alpha amylase works on the interior of starch molecules, while beta amylase acts on the ends of starch molecules. Overall, alpha amylase is more versatile in breaking down different types of starch, while beta amylase has a more specific role in starch degradation.
Beta amylase and alpha amylase are enzymes that break down starch, but they have different functions and roles. Alpha amylase breaks down starch into smaller sugar molecules, while beta amylase specifically breaks down the starch at the ends of the molecule. Alpha amylase works quickly and is active at a wide range of temperatures, while beta amylase works more slowly and is active at lower temperatures. Overall, alpha amylase plays a more significant role in starch degradation compared to beta amylase.
Proteins can form structures such as a helix or a sheet due to the specific arrangement of amino acids in their sequence. The hydrogen bonding between the amino acids in the polypeptide chain determines the secondary structure of the protein, leading to the formation of helices and sheets.