What chemical feature in the protein dictates the local secondary structure?
α-helix
β-pleated sheet
random coils
amino acid sequence
pH
hydrogen bonding
the primary structure consisted of beta-pleated sheet..so the secondary structure is where the structure coiled and characterized by an alpha-helix. i don't about random coils...
i chose hydrogen bond but its wrong..so its alpha helix....
It is not alpha helix
it should be..
or both..alpha helix and hydrogen bond
Nope. just checked. though there might be a third correct answer...
Can anybody get correct answer for this question?
The chemical feature in a protein that dictates the local secondary structure is the arrangement of amino acids and the hydrogen bonding between them.
To understand this, you need to know that proteins are made up of long chains of amino acids that are connected by peptide bonds. The primary structure of a protein is simply the linear sequence of these amino acids. However, proteins can fold into more complex structures that are determined by their primary structure.
Two common types of local secondary structures in proteins are α-helices and β-pleated sheets. These structures are stabilized by hydrogen bonds between the amino acids. In an α-helix, the hydrogen bonds form between the carbonyl group of one amino acid and the amino group of another, creating a helical structure. In a β-pleated sheet, the hydrogen bonds form between amino acids in adjacent strands, creating a sheet-like structure.
On the other hand, random coils refer to regions of the protein that do not adopt a specific secondary structure and lack regular hydrogen bonding patterns.
The specific amino acid sequence determines the potential for secondary structures to form. Certain amino acids have a greater propensity for forming α-helices or β-pleated sheets. For example, amino acids with small side chains, such as alanine or glycine, tend to favor α-helix formation. Amino acids with bulkier side chains, like valine or isoleucine, are more likely to form β-pleated sheets.
In addition to amino acid sequence, other factors such as pH and temperature can influence the stability of secondary structures. Changes in pH can affect the charge distribution in the protein, altering its folding behavior. However, pH primarily affects the overall protein structure rather than dictating the specific local secondary structures. Hydrogen bonding, which is crucial for stabilizing secondary structures, is influenced by pH.
To summarize, the amino acid sequence and the hydrogen bonding potential between amino acids are key determinants of the local secondary structure in a protein. pH and other factors can influence the stability of these structures, but they do not directly dictate the specific secondary structures.