Arginine relative hydrophobicity

Thien et al. (18) also showed that the degree of solubilisation depends on the relative hydrophobicities of the amino acid residues. A measure of this effect is the slope of the solubilisation curve when replotted as a function of the net solute charge, as shown in Figure 10 for arginine. It was found that this slope correlated well with the hydrophobicity scale proposed by Bull and Breese (1j)), as is evident from Figure 11. It is intriguing to note that the more hydrophobic the residue the greater the solubilisation of the amino acid. This could be due to one of three effects, as discussed below. 

Histone methylation participates in the regulation of gene expression patterns. Unlike histone acetylation, histone methylation does not alter the charge of the amino acid and hence the histone tail. There are changes in the basicity and the hydrophobicity which are relatively small when viewed at the scale of the histone but still influence the affinity of the histone tails to certain proteins, for example transcription factors, which in turn result in certain signaling events. The histone methyltransferases are usually subdivided into three classes SET domain lysine methyltransfeases, nonSET domain lysine methyltransferases and arginine methyltransferases (PRMTs). All of them utilize S-adenosylmethionine (SAM) as cosubstrate for the methylation reaction... 

The interactions between labeled PAMAM dendrimers (Gn-T) and amino acids and proteins, were studied with the biomolecules selected on the basis of acid-base properties. The protonated dendrimers, which are acidic, interact well with the basic Arginine. The relatively strong interactions with the hydrophobic Leucine indicated a synergistic effect between hydrophilic and hydrophobic interactions. The ESE spectra confirmed the results obtained from CW ESR, since the protons of Leucine reside in vicinity of the nitroxide group. 

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