Search results
Results from the WOW.Com Content Network
Since the asparagine side-chain can form hydrogen bond interactions with the peptide backbone, asparagine residues are often found near the beginning of alpha-helices as asx turns and asx motifs, and in similar turn motifs, or as amide rings, in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions that would ...
The strand order in this barrel (GFP) is: 1 6 5 4 9 8 7 10 11 3 2. The inter-strand hydrogen bonds can be summarised in a table. Each column contains the residues in one strand (strand 1 is repeated in the last column). The arrows indicate the hydrogen bonds that were identified in the figures.
Chemical formula: C 4 H 8 N 2 O 3 Molar mass: 132.118 g·mol −1 Systematic name: (2S)-2-amino-3-carbamoyl-propanoic acid Abbreviations: N, Asn Synonyms: (S)-2-aminosuccinic acid 4-amide {α/2}-aminosuccinamic acid Agedoite Altheine Asparagine acid Asparamide Asparatamine Aspartamic acid Aspartamine Aspartic acid β-amide Aspartic acid amide ...
The hydrophobic effect is the desire for non-polar molecules to aggregate in aqueous solutions in order to separate from water. [22] This phenomenon leads to minimum exposed surface area of non-polar molecules to the polar water molecules (typically spherical droplets), and is commonly used in biochemistry to study protein folding and other ...
Potassium asparaginate is a potassium salt of L-asparagine amino acid. [2] [3] [4] [5]Potassium asparaginate can be considered both a salt and a coordination complex. [6] [3] As a salt, potassium asparaginate is formed when the potassium ion (K +) replaces the hydrogen ion (H +) in the carboxyl group of L-asparagine, an amino acid; in this process, the carboxyl group (–COOH) in L-asparagine ...
In nonpolar solvents contact ion pairs with very high association constants are formed; [3] [4] in the gas phase the association energies of e.g. alkali halides reach up to 200 kJ/mol. [5] The Bjerrum or the Fuoss equation describe ion pair association as function of the ion charges zA and zB and the dielectric constant ε of the medium; a ...
The N-terminal residue of the intein domain must be a serine, threonine or cysteine, and it attacks its preceding peptide bond in order to form an ester or a thioester. The first residue of the second portion of the extein must be a serine, threonine or cysteine as well, and this second nucleophile forms a branched intermediary.
The "B" form described by James D. Watson and Francis Crick is believed to predominate in cells. [2] James D. Watson and Francis Crick described this structure as a double helix with a radius of 10 Å and pitch of 34 Å, making one complete turn about its axis every 10 bp of sequence. [3]