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)
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
Secondary structure is defined by hydrogen bonding, so the exact definition of a hydrogen bond is critical. The standard hydrogen-bond definition for secondary structure is that of DSSP, which is a purely electrostatic model. It assigns charges of ±q 1 ≈ 0.42e to the carbonyl carbon and oxygen, respectively, and charges of ±q 2 ≈ 0.20e to ...
The atoms in a peptide link all lie on the same plane. The nitrogen, hydrogen, and oxygen atoms in a hydrogen bond are approximately in a straight line. The carbon-oxygen and nitrogen-hydrogen groups are all involved in bonding.
The first ribbon diagrams, hand-drawn by Jane S. Richardson in 1980 (influenced by earlier individual illustrations), [3] were the first schematics of 3D protein structure to be produced systematically. [3] [4] They were created to illustrate a classification of protein structures for an article in Advances in Protein Chemistry [5] (now ...
For example, residue i may form hydrogen bonds to residues j − 1 and j + 1; this is known as a wide pair of hydrogen bonds. By contrast, residue j may hydrogen-bond to different residues altogether, or to none at all. The hydrogen bond arrangement in parallel beta sheet resembles that in an amide ring motif with 11 atoms.
Oxygen atoms are shown in red and nitrogen in blue; dotted lines represent hydrogen bonds. R groups represent the amino acid side chains. A stick representation of a peptide chain in an alpha-sheet configuration. Alpha sheet (also known as alpha pleated sheet or polar pleated sheet) is an atypical secondary structure in proteins, first proposed ...
Arginine residues interact with the nucleic acid phosphate backbone and commonly form hydrogen bonds with the base residues, particularly guanine, in protein–DNA complexes. Lysine residues can be singly, doubly and even triply methylated. Methylation does not alter the positive charge on the side chain, however. acetylation