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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 the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone N−H group hydrogen ...
Handedness (or chirality) is a property of the helix, not of the perspective: a right-handed helix cannot be turned to look like a left-handed one unless it is viewed in a mirror, and vice versa. Two types of helix shown in comparison. This shows the two chiralities of helices. One is left-handed and the other is right-handed.
In humans, chirality (also referred to as handedness or laterality) is an attribute of humans defined by their unequal distribution of fine motor skill between the left and right hands. An individual who is more dexterous with the right hand is called right-handed, and one who is more skilled with the left is said to be left-handed.
Left hands make up over 90% of the artwork, demonstrating the prevalence of right-handedness. [1] A student writes with their left hand. In human biology, handedness is an individual's preferential use of one hand, known as the dominant hand, due to it being stronger, faster or more dextrous.
Such a clustering is alternatively described in the ABEGO system, where each letter stands for α (and 3 10) helix, right-handed β sheets (and extended structures), left-handed helixes, left-handed sheets, and finally unplottable cis peptide bonds sometimes seen with proline; it has been used in the classification of motifs [14] and more ...
Handedness in and of itself tends to be a grey area. The requirements for someone to be right- as opposed to left-handed have been debated, and because individuals who identify as left-handed may also use their right hand for a large number of tasks, identifying two clearcut groups of subjects is a challenging task.
Hydrophobicity scales can also be obtained by calculating the solvent accessible surface areas for amino acid residues in the expended polypeptide chain [22] or in alpha-helix and multiplying the surface areas by the empirical solvation parameters for the corresponding types of atoms. [3]
Figure 1: The classic example of a coiled coil is the GCN4 leucine zipper (PDB accession code 1zik), which is a parallel, left-handed homodimer. However, many other types of coiled coil exist. A coiled coil is a structural motif in proteins in which 2–7 [1] alpha-helices are coiled together like the strands