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Tertiary structure While the secondary structure of proteins is determined by the interactions between amino groups and carboxylic acid groups of neighboring (but not adjacent) amino acids, tertiary structure is defined by how the R-groups of neighboring amino acids interact. These interactions result in very specific folding patterns eventually helping to stabilize a specific 3-dimensional structure of the polypeptide. Several types of interactions occur between neighboring R-groups to create the physical 3-dimensional structure of a polypeptide. Hydrogen bonding While the hydrogen bonding determines the secondary structure of proteins, hydrogen bonding can also occur between the R-groups of a polypeptide chain. The 20 R-groups of amino acids are either polar or non-polar. Polar R-groups have oxygen or nitrogen atoms which characteristically have high electronegativity due to their high affinity for electrons. These polar R-groups tend to bond with hydrogen atoms of neighboring non-polar R-groups or the amino hydrogen of the peptide backbone. Likewise, non-polar R-groups have a lack of affinity for electrons and can form hydrogen bonds with neighboring polar R-groups or the oxygen of the carboxylic acid group (or the nitrogen of the amino group) of the peptide backbone. While hydrogen bonding is relatively weak, the overarching abundance of these interactions forms very stable polypeptide structures. Hydrophobic and hydrophilic interactions All proteins are surrounded by water within the cell. Polar R-groups are hydrophilic and bend to turn towards the water; whereas non-polar R-groups are hydrophobic and turn away from water. Hydrophobic R-groups tend to amass in the internal section of the protein forming globular masses. lonic bonding While hydrogen bonding is facilitated by the interactions of partial charges, certain R-groups have full charges and are involved in ionic bonding. Ionic bonding happens between completely positive R-groups with neighboring R-groups that are completely negative. Quaternary structure The overall structure of a fully-functional protein is known as the quaternary structure. Most proteins are composed of several polypeptides. A polypeptide is composed of either a series of (alpha)-helices with tertiary level interactions, or a series of (eta)-pleated sheets with tertiary level interactions. 12. How does hydrogen bonding differ in secondary and tertiary protein structure?

Tertiary structure
While the secondary structure of proteins is determined by the interactions between amino
groups and carboxylic acid groups of neighboring (but not adjacent) amino acids, tertiary structure
is defined by how the R-groups of neighboring amino acids interact. These interactions result in
very specific folding patterns eventually helping to stabilize a specific 3-dimensional structure of
the polypeptide. Several types of interactions occur between neighboring R-groups to create the
physical 3-dimensional structure of a polypeptide.
Hydrogen bonding
While the hydrogen bonding determines the secondary structure of proteins, hydrogen bonding
can also occur between the R-groups of a polypeptide chain. The 20 R-groups of amino acids are
either polar or non-polar. Polar R-groups have oxygen or nitrogen atoms which characteristically
have high electronegativity due to their high affinity for electrons. These polar R-groups tend to
bond with hydrogen atoms of neighboring non-polar R-groups or the amino hydrogen of the
peptide backbone. Likewise, non-polar R-groups have a lack of affinity for electrons and can form
hydrogen bonds with neighboring polar R-groups or the oxygen of the carboxylic acid group (or the
nitrogen of the amino group) of the peptide backbone. While hydrogen bonding is relatively weak,
the overarching abundance of these interactions forms very stable polypeptide structures.
Hydrophobic and hydrophilic interactions
All proteins are surrounded by water within the cell. Polar R-groups are hydrophilic and bend to
turn towards the water; whereas non-polar R-groups are hydrophobic and turn away from water.
Hydrophobic R-groups tend to amass in the internal section of the protein forming globular
masses.
lonic bonding
While hydrogen bonding is facilitated by the interactions of partial charges, certain R-groups have
full charges and are involved in ionic bonding. Ionic bonding happens between completely positive
R-groups with neighboring R-groups that are completely negative.
Quaternary structure
The overall structure of a fully-functional protein is known as the quaternary structure. Most
proteins are composed of several polypeptides. A polypeptide is composed of either a series of (alpha)-helices with tertiary level interactions, or a series of (eta)-pleated sheets with tertiary level
interactions.
12. How does hydrogen bonding differ in secondary and tertiary protein structure?

Added by Leslie W.

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