Thermodynamics Of alpha-Helix Formation.
The alpha-helix was the first proposed and experimentally confirmed secondary structure. The elegant simplicity of the alpha-helical structure, stabilized by hydrogen bonding between the backbone carbonyl oxygen and the peptide amide four residues away, has captivated the scientific community. In proteins, alpha-helices are also stabilized by the so-called capping interactions that occur at both the C- and the N-termini of the helix. This chapter provides a brief historical overview of the thermodynamic studies of the energetics of helix formation, and reviews recent progress in our understanding of the thermodynamics of helix formation.
Makhatadze
George I
GI
Department of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, Pennsylvania 17033.
D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D013816:Thermodynamics
D011506:Proteins