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The chair conformation of six-membered rings have a dihedral angle of 60° between adjacent substituents thus usually making it the most stable conformer. Since there are two possible chair conformation steric and stereoelectronic effects such as the anomeric effect, 1,3-diaxial interactions, dipoles and intramolecular hydrogen bonding must be taken into consideration when looking at relative ...
The primary structure of a protein, its linear amino-acid sequence, determines its native conformation. [11] The specific amino acid residues and their position in the polypeptide chain are the determining factors for which portions of the protein fold closely together and form its three-dimensional conformation.
A conformational epitope is formed by the 3-D conformation adopted by the interaction of discontiguous amino acid residues. In contrast, a linear epitope is formed by the 3-D conformation adopted by the interaction of contiguous amino acid residues. A linear epitope is not determined solely by the primary structure of the involved amino acids.
A Haworth projection has the following characteristics: [3] Carbon is the implicit type of atom. In the example on the right, the atoms numbered from 1 to 6 are all carbon atoms. Carbon 1 is known as the anomeric carbon. Hydrogen atoms on carbon are implicit. In the example, atoms 1 to 6 have extra hydrogen atoms not depicted.
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.
Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a ...
Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [1] The two most common secondary structural elements are alpha helices and beta sheets , though beta turns and omega loops occur as well.
In the chair and skew conformations, the reference plane should be selected. In the chair conformation, the reference plane is chosen such that the lowest-numbered atom (usually C-1) is exoplanar. In the skew conformation, the plane contains three adjacent atoms and one other with the atom with the lowest possible number exoplanar. [6]