Alpha helix - Wikipedia
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 .
Secondary Structure: α-Helices - Chemistry LibreTexts
An α-helix is a right-handed coil of amino-acid residues on a polypeptide chain, typically ranging between 4 and 40 residues. This coil is held together by hydrogen bonds between the oxygen of C=O on top coil and the hydrogen of N-H on the bottom coil.
Secondary Structure (2˚) -- Alpha Helices - University of Vermont
An alpha helix is an element of secondary structure in which the amino acid chain is arranged in a spiral. The kinemage linked above shows an individual alpha helix, viewed from the N-terminal end to resemble the "helical wheel" (see figure below).
Design of complicated all-α protein structures | Nature Structural ...
2024年1月4日 · In this article, we sought to develop a computational method to design complicated all-α structures by employing helix–loop–helix (HLH) motifs typically observed in naturally occurring...
7.4: Secondary structure of proteins - Chemistry LibreTexts
2023年9月21日 · The two common secondary structures encountered in proteins are (\(\alpha\)-helix and \(\beta\)-pleated sheet. The other portions of the polymer backbone that are regular but not repetitive are called random coils. Triple-helix is another common secondary structure found in collagen proteins in connective tissues.
Four Types of Protein Structure - ThoughtCo
2024年7月26日 · One type is the alpha (α) helix structure. This structure resembles a coiled spring and is secured by hydrogen bonding in the polypeptide chain. The second type of secondary structure in proteins is the beta (β) pleated sheet.
26.10: Protein Structure - Chemistry LibreTexts
In a helix, the main chain of the protein adopts the shape of a clockwise spiral staircase, and the side chains point out laterally. In a beta-sheet (or beta-strand) structure, two sections of protein chain are aligned side-by-side in an extended conformation.
Understanding a protein fold: The physics, chemistry, and biology …
2023年4月1日 · α-Helix and coiled-coil geometry. A, the α helix has a rise per residue (r) of 1.5 Å, 3.6 residues per helical turn, a backbone radius of 2.3 Å, and is stabilized by i CO to i + 4 NH hydrogen bonds. B, in Crick’s helical nets, the positions of the Cα atoms of an α helix, are projected as points onto a 2D plot (red).
Structure and Stability of the α-Helix | SpringerLink
Here we discuss structural features that are important for designing peptide helices, including amino acid preferences for interior and terminal positions, side chain interactions, disulfide bonding, metal binding, and phosphorylation.
The Structure of α-Helical Coiled Coils - ScienceDirect
2005年1月1日 · α-Helical coiled coils are versatile protein domains, supporting a wide range of biological functions. Their fold is probably better understood than that of any other protein; indeed, uniquely among folds, their structure can be computed from a set of parametric equations.