The E2A gene encodes two alternatively spliced products, E12 and E47. The two proteins differ in their basic helix-loop-helix motifs (bHLH), responsible for DNA binding and dimerization. Although both E12 and E47 can bind to DNA as heterodimers with tissue-specific bHLH proteins, E12 binds to DNA poorly as homodimers. An inhibitory domain in E12 has previously been found to prevent E12 homodimers from binding to DNA. By measuring the dissociation rates using filter binding and electrophoretic mobility shift assays, we have shown here that the inhibitory domain interferes with DNA binding by destabilizing the DNA-protein complexes. Furthermore, we have demonstrated that substitution of basic amino acids (not other amino acids) in the DNA-binding domain of E12 can increase the intrinsic DNA-binding activity of E12 and stabilize the binding complexes, thus alleviating the repression from the inhibitory domain. *This ability of basic amino acids to stabilize DNA-binding complexes may be of biological significance in the case of myogenic bHLH proteins, which all possess two more basic amino acids in their DNA binding domain than E12.* To function as heterodimers with E12, the myogenic bHLH proteins may need stronger DNA binding domains. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=145871 Helix-capping interactions were found to contribute to helix stability, even when the substitution site was not at the end of the peptide- the H-bonds. BETA TURN. Many antiparallel beta sheets are formed by a single peptide chain continually looping back on itself. The loop between the two hydrogen-bonded segments, known as a beta turn, consistently contains one to three (usually two) amino acids. The amino acids in a beta turn do not form hydrogen bonds, but other interactions may stabilize their positions. A further consistency is that, from a perspective where the side chain of the final hydrogen-bonded amino acid projects outward toward the viewer, the turn is always to the right. http://science.jrank.org/pages/5539/Proteins.html -that is a good website
From a nucleic acid code to an amino acid code
A beta-amino acid is an amino acid which has the amino and carboxylic functional groups attached to adjacent carbon atoms.
amino acid
The pitch of a helix is defined as the distance along the helical axis that results in one full turn of the helix. In the case of amino acid helices, this value is an average value of about 5.5 Angstroms. A-DNA B-DNA Z-DNA Right-handed helix Right-handed Left-handed Short and broad Long and thin Longer and thinner Helix Diameter 25.5A 23.7A 18.4A Rise / base-pair 2.3A 3.4A 3.8A Base-pair / helical turn ~ 11 ~ 10 ~ 12 Helix pitch 25A 34A 47A Tilt of the bases 20 deg -1 deg -9 deg Also see http://tigger.uic.edu/classes/phys/phys461/phys450/ANJUM04/
limiting amino acid
3.6 amino acid.
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proline is not an amino acid it is an imino acid
In an α-helix, the polypeptide backbone forms a repeating helical structure that is stabilized by hydrogen bonds between a carbonyl oxygen and an amine hydrogen. These hydrogen bonds occur at regular intervals of one hydrogen bond every fourth amino acid and cause the polypeptide backbone to form a helix.
Codons are sequences of three nucleotides that connect the double stranded helix of DNA which are described as "ladder rungs" and they each call for a specific amino acid.
amino acid
From a nucleic acid code to an amino acid code
A beta-amino acid is an amino acid which has the amino and carboxylic functional groups attached to adjacent carbon atoms.
Nope. To my knowledge there are only two acidic amino acids: Aspartic acid and glutamic acid.
Glycogenic amino acid is an amino acid that can be converted into glycogen bodies throught glycogenesis
non polar bond
aromatic amino acid