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methyl is hydrophobic because it is non polar. the c-h bonds have little electronegativity difference I believe. water is polar, and nonpolar things don't tend to react or dissolve in polar substances.

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17y ago

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What is the R group found in alanine?

The R group in alanine is a simple methyl group (CH3). This nonpolar, hydrophobic side chain is small and uncharged, making alanine a neutral, aliphatic amino acid.


What 2 4?

CH3-C(CH3)2-CH3-C(CH3)2-CH3 , 2,2,4,4-tetramethyl pentane


What’s 2×4?

CH3-C(CH3)2-CH3-C(CH3)2-CH3 , 2,2,4,4-tetramethyl pentane


What is the correct structure of 3-ethyl-3-methylhexane?

The correct structure of 3-ethyl-3-methylhexane is: CH3-CH2-CH(CH3)-CH2-CH(CH3)-CH3


What is the name for the CH3-Ch-CH3 alkyl group?

The name for the CH3-Ch-CH3 alkyl group is isopropyl.


What is the extended structural formula of 2-methyl propane?

Difficult to draw here, but let's try to describe: Three methyl groups (CH3-) and one H- atom bonded to one central C atom, then you'll get something like this: . . . .H CH3-C-CH3 . . . .CH3


How do you name this molecule ch3 ch2 ch3?

CH3-CH2-CH3 is a gas Propane.


Can you make two structural isomers from a saturated alkane C4H10?

n-butane CH3-CH2-CH2-CH3 and isobutane CH3-CH(CH3)-CH3


what is the formula for "2-bromo-2-methylpropane + H2O →2-methylpropan-2-ol + HBr"?

CH3-C(Br)(CH3)-CH3 + H2O = CH3-C(OH)(CH3)-CH3 + HBr


What is condensed formula for 2 3 3 4 tetramethylnonane?

The condensed formula for 2,3,3,4-tetramethylnonane is CH3-CH(CH3)-CH(CH3)-CH2-CH2-CH2-CH2-CH2-CH3.


What is the structure of 2-pentanone?

CH3-CH(=O)-CH(CH3)-CH2-CH3


The r group or side chain of the amino acid serine is -ch2-oh the r group or side chain of the amino acid alanine is -ch3 where would you expect to find these amino acids in a globular protein in aq?

Serine, being hydrophilic, will be more likely to appear near the surface of a globular protein in solution, and alanine, being hydrophobic, will more likely appear near the centre of the protein. This illustrates the "hydrophobic effect", which is one of the effects that stabilizes the tertiary and quaternary structures of proteins. The hydrophobic effect is not due to an intramolecular force but the tendency of hydrophilic and hydrophobic amino acids to interact oppositely with water and segregate into surface and inner regions.