Picture attached to help answer question. 1) In the hydrophobicity scale, tyrosi
ID: 145982 • Letter: P
Question
Picture attached to help answer question.1) In the hydrophobicity scale, tyrosine, a polar, uncharged amino acid, turned out to have a significantly greater hydrophobicity (ranked 5 in your scale) than glycine, a nonpolar amino acid (ranked 11 in your scale. Explain this based on a comparison of the structure / chemistry of the structures of these two amino acids. Be very specific in describing structures / chemistry. Table 2. Hydrophobicity Scales Fig 2. Comparison of Hydrophobicity Scales Engleman et CellBiolOLM Class Scale Correlation Coefficient (g) 0.7473 Group Nonpolar Charged Amino Acid al. Scale 1.6 0.510 0.800 0.353 Aspartic Acid Unc 0.600 0.358 8.2 4.1 Acid Nonpolar 0.376 0.400 0.732 Nonpolar Charged 8.8 349 0 200 Nonpolar 3.7 0.6 0,461 0.000 14 105 3.5 3.5 0.7 0.574 Engleman et al Scale Valine Scatter plot of Eneleman bydrophobicity scale data vs. Cell Biology class data, both taken from table 2 data, both taken from table 2
Explanation / Answer
Tyrosine is polar molecule but partially hydrophobic in nature . This is because tyrosine has large aromatic ring and also OH group. The oxygen in the OH group involves in producing dipole . Thus the molecule is polar but yet it exhibits slight hydrophic. The polar OH also forms hydrogen bonding with water. Glycine is not neither hydrophilic nor hydrophobic. It doesnot have side chains. It has only one Hydrogen group. That is why it can fit in any hydrphobic or hydrophilic environment. This property of glycine makes it unique aminoacid. Because of this reason tyrosine has greater hydrophobicity than glycine.