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doi: 10.1007/s13555-013-0026-x

In the MD studies, weaker interactions of oxyntomodulin with residues deep in the cavity, particularly R190 2.60 , were coupled with a loss of stable interactions along the entire face of the TM2 helix and weaker interactions with ECL2, all of which interact with the same face of the helical GLP-1 peptide (Fig