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    Causes of Hydrophobic Interactions

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    Lucky Lokesh
    Hydrophobic interactions occur between nonpolar molecules and water. Hydrophobes are not soluble in water and tend to cluster together to minimize contact with water molecules. This clustering is driven by thermodynamics - when hydrophobes come together in water, entropy increases as fewer water molecules need to be reoriented around each hydrophobe. This entropic gain makes hydrophobic interactions spontaneous despite any enthalpic costs. Hydrophobic interactions are important for protein folding and structure, allowing nonpolar residues to cluster inside the protein core while polar residues interact with the surrounding water.

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    Causes of Hydrophobic Interactions

    Uploaded by

    Lucky Lokesh
    40 views3 pages
    Hydrophobic interactions occur between nonpolar molecules and water. Hydrophobes are not soluble in water and tend to cluster together to minimize contact with water molecules. This clustering is driven by thermodynamics - when hydrophobes come together in water, entropy increases as fewer water molecules need to be reoriented around each hydrophobe. This entropic gain makes hydrophobic interactions spontaneous despite any enthalpic costs. Hydrophobic interactions are important for protein folding and structure, allowing nonpolar residues to cluster inside the protein core while polar residues interact with the surrounding water.

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    Hydrophobic_Interactions

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    Hydrophobic interactions occur between nonpolar molecules and water. Hydrophobes are not soluble in water and tend to cluster together to minimize contact with water molecules. This clustering is driven by thermodynamics - when hydrophobes come together in water, entropy increases as fewer water molecules need to be reoriented around each hydrophobe. This entropic gain makes hydrophobic interactions spontaneous despite any enthalpic costs. Hydrophobic interactions are important for protein folding and structure, allowing nonpolar residues to cluster inside the protein core while polar residues interact with the surrounding water.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    40 views3 pages

    Causes of Hydrophobic Interactions

    Uploaded by

    Lucky Lokesh
    Hydrophobic interactions occur between nonpolar molecules and water. Hydrophobes are not soluble in water and tend to cluster together to minimize contact with water molecules. This clustering is driven by thermodynamics - when hydrophobes come together in water, entropy increases as fewer water molecules need to be reoriented around each hydrophobe. This entropic gain makes hydrophobic interactions spontaneous despite any enthalpic costs. Hydrophobic interactions are important for protein folding and structure, allowing nonpolar residues to cluster inside the protein core while polar residues interact with the surrounding water.

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    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
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    of 3

    Hydrophobic Interactions

    Hydrophobic interactions describe the relations between water and hydrophobes (low water-soluble molecules).
    Hydrophobes are nonpolar molecules and usually have a long chain of carbons that do not interact with water molecules.
    The mixing of fat and water is a good example of this particular interaction. The common misconception is that water and
    fat doesn’t mix because the Van der Waals forces that are acting upon both water and fat molecules are too weak.
    However, this is not the case. The behavior of a fat droplet in water has more to do with the enthalpy and entropy of the
    reaction than its intermolecular forces.

    Causes of Hydrophobic Interactions


    American chemist Walter Kauzmann discovered that nonpolar substances like fat molecules tend to clump up together
    rather than distributing itself in a water medium, because this allow the fat molecules to have minimal contact with water.

    The image above indicates that when the hydrophobes come together, they will have less contact with water. They interact
    with a total of 16 water molecules before they come together and only 10 atoms after they interact.

    Thermodynamics of Hydrophobic Interactions


    When a hydrophobe is dropped in an aqueous medium, hydrogen bonds between water molecules will be broken to make
    room for the hydrophobe; however, water molecules do not react with hydrophobe. This is considered an endothermic
    reaction, because when bonds are broken heat is put into the system. Water molecules that are distorted by the presence of
    the hydrophobe will make new hydrogen bonds and form an ice-like cage structure called a clathrate cage around the
    hydrophobe. This orientation makes the system (hydrophobe) more structured with an decrease of the total entropy of the
    system; therefore ΔS < 0 .

    The change in enthalpy (ΔH ) of the system can be negative, zero, or positive because the new hydrogen bonds can
    partially, completely, or over compensate for the hydrogen bonds broken by the entrance of the hydrophobe. The change in
    enthalpy, however, is insignificant in determining the spontaneity of the reaction (mixing of hydrophobic molecules and
    water) because the change in entropy (ΔS ) is large.
    According to the Gibbs Energy formula

    ΔG = ΔH − T ΔS (1)

    1 12/25/2021 https://chem.libretexts.org/@go/page/1506
    with a small unknown value of ΔH and a large negative value of ΔS , the value of ΔG will turn out to be positive. A
    positive ΔG indicates that the mixing of the hydrophobe and water molecules is not spontaneous.

    Formation of Hydrophobic Interactions


    The mixing hydrophobes and water molecules is not spontaneous; however, hydrophobic interactions between
    hydrophobes are spontaneous. When hydropobes come together and interact with each other, enthalpy increases ( ΔH is
    positive) because some of hydrogen bonds that form the clathrate cage will be broken. Tearing down a portion of the
    clathrate cage will cause the entropy to increase ( ΔS is positive), since forming it decreases the entropy.
    According to the Equation 1
    ΔH = small positive value
    ΔS = large positive value
    Result: ΔG is negative and hence hydrophobic interactions are spontaneous.

    Strength of Hydrophobic Interactions


    Hydrophobic interactions are relatively stronger than other weak intermolecular forces (i.e., Van der Waals interactions or
    Hydrogen bonds). The strength of Hydrophobic Interactions depend on several factors including (in order of strength of
    influence):
    1. Temperature: As temperature increases, the strength of hydrophobic interactions increases also. However, at an
    extreme temperature, hydrophobic interactions will denature.
    2. Number of carbons on the hydrophobes: Molecules with the greatest number of carbons will have the strongest
    hydrophobic interactions.
    3. The shape of the hydrophobes: Aliphatic organic molecules have stronger interactions than aromatic compounds.
    Branches on a carbon chain will reduce the hydrophobic effect of that molecule and linear carbon chain can produce
    the largest hydrophobic interaction. This is so because carbon branches produce steric hindrance, so it is harder for two
    hydrophobes to have very close interactions with each other to minimize their contact to water.

    Biological Importance of Hydrophobic Interactions


    Hydrophobic Interactions are important for the folding of proteins. This is important in keeping a protein stable and
    biologically active, because it allow to the protein to decrease in surface are and reduce the undesirable interactions with
    water. Besides from proteins, there are many other biological substances that rely on hydrophobic interactions for its
    survival and functions, like the phospholipid bilayer membranes in every cell of your body!

    2 12/25/2021 https://chem.libretexts.org/@go/page/1506
    Illustration of how protein changes shape to allow polar regions (blue) to interact with water while non-polar hydrophobic
    regions (red) do not interact with the water. (CC BY-SA 3.0; Treshphrd).

    References
    1. Atkins, Peter and Julio de Paula. Physical Chemistry for the Life Sciences. Oxford, UK: Oxford University Press.
    2006. 95.
    2. Chang, Raymond. Physical Chemistry for the Biosciences. Sausalito, CA: Edwards Brothers, Inc. 2005. 508-510.
    3. Garrett, Reginald H. and Charles M. Grisham. Biochemistry. Belmont, CA: Thomas Brooks/Cole. 2005. 15.

    Contributors and Attributions


    Justin Than (UCD)

    3 12/25/2021 https://chem.libretexts.org/@go/page/1506

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