By Hans - editor Neurath
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Extra info for The Proteins Composition, Structure, and Function. Volume 4
Since reticulocytes in the process of hemoglobin synthesis contain mes› senger RNA’s with five ribosomes per molecule, it was concluded that each molecule of messenger RNA coding for a hemoglobin polypeptide chain probably contained approximately 450 nucleotides. Since each hemoglobin chain is approximately 150 amino acid residues in length, this would give a ratio of three nucleotides in the messenger per amino acid in the polypeptide chain. Very little information is available on the sequence of nucleotides within coding units.
1964). It is probably reasonable to consider all of the known noncovalent forces as participat› ing factors in the specific association of the subunits. However, as in the maintenance of the tertiary structure of a single polypeptide chain, the present evidence indicates a more important role for hydrophobic bonding than for hydrogen bonding, or for electrostatic forces (Schachman, 1963). 2. Site of Assembly of Multichain Proteins Although the in vitro studies clearly support the hypothesis which states that the unique association of protein subunits is an inherent property of the amino acid sequences of the polypeptide chain, there remain a number of unanswered questions regarding the organization of these subunits.
Thus, plus and minus appeared to represent two very different types of alterations in the genetic mate› rial. The two categories were interpreted by Crick et al. (1961) as insertions and deletions of single nucleotides. If the code were triplet and read from a fixed starting point, three nucleotides at a time, the effect of a single nucleotide deletion could be reversed by adding a nucleotide at the original position, or possibly by adding a nucleotide at another position in the same gene. The amino acids in-between the two points of mutation in the plus-minus strain probably would not be the same as in the unmutated protein.
The Proteins Composition, Structure, and Function. Volume 4 by Hans - editor Neurath