Hydrogen Bonding Information Sheet Template Page 3

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Proteins
Hydrogen bonding is present abundantly in the secondary structure of proteins, and also sparingly in tertiary
conformation. The secondary structure of a protein involves interactions (mainly hydrogen bonds) between neighboring
polypeptide backbones which contain Nitrogen-Hydrogen bonded pairs and oxygen atoms. Since both N and O are
strongly electronegative, the hydrogen atoms bonded to nitrogen in one polypeptide backbone can hydrogen bond to
the oxygen atoms in another chain and visa-versa. Though they are relatively weak,these bonds offer great stability to
secondary protein structure because they repeat a great number of times.
In tertiary protein structure, interactions are primarily between functional R groups of a polypeptide chain; one such
interaction is called a hydrophobic interaction. These interactions occur because of hydrogen bonding between water
molecules around the hydrophobe and further reinforce conformation.
References
1. Brown, et al. Chemistry:The Central Science. 11th ed. Upper Saddle River, New Jersey: Pearson/Prentice Hall,
2008.
2. Chang, Raymond. General Chemistry:The Essential Concepts. 3rd ed. New York: Mcgraw Hill, 2003
3. Petrucci, et al. General Chemistry: Principles & Modern Applications. 9th ed. Upper Saddle River, New Jersey:
Pearson/Prentice Hall, 2007.
Contributors
Jose Pietri (UCD)
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