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A protein backbone hydrogen bond incompletely shielded from water attack is a dehydron. Dehydrons promote the removal of water through proteins or ligand binding. The exogenous dehydration enhances the electrostatic interaction between the amide and carbonyl groups by de-shielding their partial charges.
If the helix or sheet hydrogen bonding pattern is too short they are designated as T or B, respectively. Other protein secondary structure assignment categories exist (sharp turns, Omega loops, etc.), but they are less frequently used. Secondary structure is defined by hydrogen bonding, so the
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)
The β pleated sheet is a structure that forms with the backbone bending over itself to form the hydrogen bonds (as displayed in the figure to the left). The hydrogen bonds are between the amide hydrogen and carbonyl oxygen of the peptide bond. There exists anti-parallel β pleated sheets and parallel β pleated sheets where the stability of ...
The free energy of stabilization of soluble globular proteins typically does not exceed 50 kJ/mol. [citation needed] Taking into consideration the large number of hydrogen bonds that take place for the stabilization of secondary structures, and the stabilization of the inner core through hydrophobic interactions, the free energy of ...
DSSP begins by identifying the intra-backbone hydrogen bonds of the protein using a purely electrostatic definition, assuming partial charges of −0.42 e and +0.20 e to the carbonyl oxygen and amide hydrogen respectively, their opposites assigned to the carbonyl carbon and amide nitrogen.
Most importantly, the N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid five residues earlier; this repeated i + 5 → i hydrogen bonding defines a π-helix. Similar structures include the 3 10 helix (i + 3 → i hydrogen bonding) and the α-helix (i + 4 → i hydrogen bonding). Top view of the same helix ...
The main chain–main chain hydrogen bond is replaced by a side chain–main chain hydrogen bond. 3D computer superimposition shows that, in proteins, they occur [12] as one of the same four types that beta turns do, except that their relative frequency of occurrence differs: type II’ is the most common, followed by types I, II and I’.