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Cover Image, Volume 36, Issue 10
Publication year - 2015
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.23901
Subject(s) - peptide , cover (algebra) , citation , volume (thermodynamics) , chemistry , computer science , molecule , hydrogen bond , physics , library science , thermodynamics , biochemistry , organic chemistry , engineering , mechanical engineering
Constraining a peptide‐based drug with a hydrocarbon chain ‐ in a process known as stapling ‐ changes the overall chemical properties of the peptide‐protein interface. When the peptide gradually approaches its target, the hydrophobic staple may kinetically trap a chain of water molecules that have to be released upon binding. In the report on page 773 (DOI: 10.1002/jcc.23859 ), Adelene Y. L. Sim and Chandra Verma report the favorable hydrogen bonding interactions between the water molecules, peptide, and protein could reduce the transition state energy barrier, thereby altering the kinetic properties of peptide binding.