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Domain A, the larger of the two domains, contains residues 1-17 and 90–194 in TSST-1 and consists of a long alpha (α) helix with residues 125-140 surrounded by a 5-strand beta (β) sheet. [ 1 ] [ 5 ] Domain B is unique because it contains residues 18–89 in TSST-1 and consists of a (β) barrel made up of 5 β-strands. [ 1 ]
Three-dimensional structure [1] of an alpha helix in the protein crambin. An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is ...
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation, radiation, or heat. [3]
A typical example is gramicidin A, a peptide that forms a dimeric transmembrane β-helix. [8] This peptide is secreted by gram-positive bacteria as an antibiotic. A transmembrane polyproline-II helix has not been reported in natural proteins. Nonetheless, this structure was experimentally observed in specifically designed artificial peptides. [9]
The helix-turn-helix motif is a DNA-binding motif. The recognition and binding to DNA by helix-turn-helix proteins is done by the two α helices, one occupying the N-terminal end of the motif, the other at the C-terminus. In most cases, such as in the Cro repressor, the second helix contributes most to DNA recognition, and hence it is often ...
The alpha helix spiral formation An anti-parallel beta pleated sheet displaying hydrogen bonding within the backbone Formation of a secondary structure is the first step in the folding process that a protein takes to assume its native structure.
The amphipathic N-terminal segment of the alpha- helix is mainly responsible for the increase in permeability of the bacterial membrane which kills the bacteria. [1] Moricin functions as an antibacterial peptide against Gram-positive and Gram-negative bacteria, with its main activity being towards Gram-positive bacteria. [1]
[26] [28] The most known SF1A helicases are Rep and UvrD in gram-negative bacteria and PcrA helicase from gram-positive bacteria. [26] The most known Helicases in the SF1B group are RecD and Dda helicases. [26] They have a RecA-like-fold core. [27] Superfamily 2 (SF2): This is the largest group of helicases that are involved in varied cellular ...