Principles of Protein Structure - H. Schultz 1982

Interactions Determining Protein Structure
Conclusion

As discussed in Chapter 1, the formation and stability of Cell/13.html">Protein Structure largely depend on non-covalent forces. These are subdivided into (1) repulsion between non-bonded atoms, (2) interactions between oscillating dipoles resulting in attractive dispersion forces, (3) electrostatic attraction and repulsion of partial charges, as well as the attraction of full charges in salt bridges, and (4) Hydrogen Bonds. Because Proteins exist exclusively in aqueous environments, the system must be considered as a whole: both the polypeptide chain and the solvent. In equation (3.2), the Entropy and bonding energy terms are treated separately. Hydrophobic forces make the largest contribution to protein stability. The high packing density observed in proteins indicates the efficient utilization of all non-covalent forces in organizing their structure. The interior of a protein is packed as densely as a good crystal.



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