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...

proposed that the 310-helix serves as an intermediary conformation of sorts, and provides insight into the initiation of α-helix folding. Max Perutz, the...

secondary structure. The secondary structure of α-keratin is very similar to that of a traditional protein α-helix and forms a coiled coil. Du it can function...

Right-handed 310 helix H = Right-handed α-helix I = Right-handed π-helix g = Left-handed 310 helix h = Left-handed α-helix i = Left-handed π-helix 3 = 310-like...

recognition. 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,...

an American biochemist, mostly known for his role in discovery of the α-helix and the β-sheet with Linus Pauling. Also working with Pauling was Herman...

hydrogen bonding defines a π-helix. Similar structures include the 310 helix (i + 3 → i hydrogen bonding) and the α-helix (i + 4 → i hydrogen bonding)...

molecular modeling and alignments. The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with...

α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as...

regular α-helix and β-sheet structure. Three left-handed helical strands twist to form a right-handed triple helix. A collagen triple helix has 3.3 residues...

heterogeneous environment for the nascent transmembrane α-helices. A relatively polar amphiphilic α-helix can adopt a transmembrane orientation in the translocon...

oscillators that is localized on the α-helix acts through a phonon coupling effect to distort the structure of the α-helix, while the helical distortion reacts...

Gly, and for Pro. The most common regions are labeled: α for α helix, Lα for left-handed helix, β for β-sheet, and ppII for polyproline II. Such a clustering...

fold formed by units composed of a short α-helix followed by two anti-parallel β-strands, followed by an α-helix and a β-strand; the three β-strands form...

Pauling in a nearly simultaneous paper. Huggins also produced a model of the α-helix in 1943, roughly eight years ahead of the modern model of Linus Pauling...

polypeptide backbone chain. Two main types of secondary structure, the α-helix and the β-strand or β-sheets, were suggested in 1951 by Linus Pauling....

_{max}={\frac {1-\sin {\phi }}{1+\sin {\phi }}}} Where α {\displaystyle \alpha \,} is the helix angle, ϕ {\displaystyle \phi \,} is the friction angle...

The Helix Nebula (also known as NGC 7293 or Caldwell 63) is a planetary nebula (PN) located in the constellation Aquarius. Discovered by Karl Ludwig Harding...

transmembrane topology. These proteins have one of two structural architectures: Helix bundle proteins, which are present in all types of biological membranes;...

and nonpolar/greasy environments. Collagen helix Foldamers Folding (chemistry) Tertiary structure α-helix Structural motif Voet D, Voet JG (2004). Biochemistry...

activity. On C-terminal part of the CAT Domain the hB α-helix, known as the "active-site helix" encompasses part of the "zinc-binding consensus sequence"...

suitable for building α-helix or β-sheet secondary structural elements. Dominant secondary structures in life as we know it are α-helices and β-sheets...

are typically spaced at 3-bp intervals. The α-helix of each domain (often called the "recognition helix") can make sequence-specific contacts to DNA...

α-helix toward the β-pleated sheet. The α-helix is flexible in closed channels. When an α-helix of a CNGA1 subunit is in close proximity to another α-helix...

The secondary structure of sTNF consists of 10 β-strands and a single α-helix. The tertiary structure consists of two antiparallel β-sheets arranged...

Hedera helix, the common ivy, European ivy, or just ivy, is a species of flowering plant in the family Araliaceae. It is native to most of Europe and...

an all-hydrocarbon cross-link for peptide α-helix stabilization, combining the principles of RCM with α,α-disubstitution of the amino acid chiral carbon...

the 16S ribosomal RNA gene, MT-RNR2. Its structure contains a three-turn α-helix, and no symmetry. In in vitro and animal models, it appears to have cytoprotective...

consists of three antiparallel β-strands followed by C- terminal α-helix and this α-helix together with the first β-strand are involved in forming a dimeric...

domain. SNAP-25 has been identified to contribute two α-helices to the SNARE complex, a four-α-helix domain complex. The SNARE complex participates in vesicle...