Abstract
The relationship between protein structure and function is the key interface between chemistry and life. The forces that dictate dynamic biochemical reactions inside cells more often involve transient weak molecular interactions than changes in covalent bonding. Just as two Lego’s are held together by collective weak forces that work synergistically because of the complementary shape of the bocks, biological macromolecules use specific shapes to organize their collective weak chemical forces to direct molecular interactions. Thus, molecular shape is a principal determinant of biochemistry. The class of biomolecules called proteins provide an extremely diverse set of shapes, which form structures conferring activities ranging from chemical catalysis to the scaffolding that structures cells (Fig.3.1). The diversity of protein structures is a direct result of the large variation in amino acid content and polymer length dictated by the coding regions of our genomes. This chapter will introduce amino acid polymerization and the forces that drive protein folding and structure.
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Further Reading
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Fromm, H.J., Hargrove, M.S. (2012). Protein Structure and Function. In: Essentials of Biochemistry. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-19624-9_3
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DOI: https://doi.org/10.1007/978-3-642-19624-9_3
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