Search results
Results from the WOW.Com Content Network
The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)
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 ]
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 and radiation, or heat. [3]
A typical example is gramicidin A, a peptide that forms a dimeric transmembrane β-helix. [7] 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. [8]
In 1951, Pauling published the structure of the alpha helix, a fundamentally important structural component of proteins. In early 1953, Pauling published a triple helix model of DNA, which subsequently turned out to be incorrect. [3] Both Crick, and particularly Watson, thought that they were racing against Pauling to discover the structure of DNA.
[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 ...
A DNA unwinding element (DUE or DNAUE) is the initiation site for the opening of the double helix structure of the DNA at the origin of replication for DNA synthesis. [1] It is A-T rich and denatures easily due to its low helical stability, [ 2 ] which allows the single-strand region to be recognized by origin recognition complex .
These methods were based on the helix- or sheet-forming propensities of individual amino acids, sometimes coupled with rules for estimating the free energy of forming secondary structure elements. The first widely used techniques to predict protein secondary structure from the amino acid sequence were the Chou–Fasman method [ 17 ] [ 18 ] [ 19 ...