The article discusses the role of multivalent interactions in chromatin transactions, where multiple binding modules on effector proteins can engage with a single histone tail or multiple tails, enhancing the specificity and affinity of chromatin interactions. The authors propose that these multivalent interactions may play a significant role in the structural and functional dynamics of chromatin, potentially resolving some of the challenges associated with the traditional view of a one-mark-to-one-module relationship. They highlight several examples of chromatin modifications and their binding partners, such as acetylation and bromodomains, methylation and chromodomains, and DNA methylation and methyltransferases. The article also explores the biophysical principles behind multivalent interactions, including thermodynamic and kinetic effects, and suggests that these interactions can enhance binding affinity and specificity while maintaining dynamic properties. The authors argue that the widespread use of multivalent recognition in chromatin biology may provide a more comprehensive framework for understanding the complex regulatory mechanisms of the genome.The article discusses the role of multivalent interactions in chromatin transactions, where multiple binding modules on effector proteins can engage with a single histone tail or multiple tails, enhancing the specificity and affinity of chromatin interactions. The authors propose that these multivalent interactions may play a significant role in the structural and functional dynamics of chromatin, potentially resolving some of the challenges associated with the traditional view of a one-mark-to-one-module relationship. They highlight several examples of chromatin modifications and their binding partners, such as acetylation and bromodomains, methylation and chromodomains, and DNA methylation and methyltransferases. The article also explores the biophysical principles behind multivalent interactions, including thermodynamic and kinetic effects, and suggests that these interactions can enhance binding affinity and specificity while maintaining dynamic properties. The authors argue that the widespread use of multivalent recognition in chromatin biology may provide a more comprehensive framework for understanding the complex regulatory mechanisms of the genome.