作者: Nir London , Dana Movshovitz-Attias , Ora Schueler-Furman
DOI: 10.1016/J.STR.2009.11.012
关键词: Peptide sequence 、 Hydrogen bond 、 Binding energy 、 Protein structure 、 Plasma protein binding 、 Signal transduction 、 Binding site 、 Biochemistry 、 Peptide 、 Biophysics 、 Chemistry
摘要: Peptide-protein interactions are very prevalent, mediating key processes such as signal transduction and protein trafficking. How can peptides overcome the entropic cost involved in switching from an unstructured, flexible peptide to a rigid, well-defined bound structure? A structure-based analysis of peptide-protein interactions unravels that most peptides do not induce conformational changes on their partner upon binding, thus minimizing the entropic cost of binding. Furthermore, peptides display interfaces that are better packed than protein …