作者: Keith K. Khoo , Raymond S. Norton
DOI: 10.1002/9783527631841.CH11
关键词:
摘要: The native structures of proteins and peptides are stabilized by a number of interactions that dictate directly or indirectly the folding, conformation, and flexibility of the molecule. Most of these interactions, such as hydrogen bonds and hydrophobic interactions, are noncovalent and relatively weak. Covalent interactions, on the other hand, are generally stronger, and are thought to exert a greater influence on stability and conformation, particularly in peptides, which tend to have fewer and weaker hydrophobic interactions because of their …