Explain the secondary structure of proteins.
Protein secondary structure is the three dimensional form of local segments of proteins.
The pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone defines the secondary structure, which is the interaction of the hydrogen bond donor and acceptor residues of the repeating peptide unit.
Before the protein folds into its three-dimensional tertiary structure, the secondary structure elements usually form spontaneously as an intermediate. The most common secondary structures are alpha-helices and beta-sheets, but beta turns and omega loops can also occur.
Multiple sequence alignment can benefit from the application of protein secondary structure.
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The local folding patterns found within a polypeptide chain, which are mainly defined by alpha-helices and beta-sheets, are referred to as the secondary structure of proteins.
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When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
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