01256nas a2200169   4500008004100000245010300041210006900144260000800213300001600221520059600237100002500833700002200858700002100880700003100901700002800932856012600960       2017                        eng d00aStructural insights into the hydrogen-bonding and folding pattern in ant-ant-pro-gly tetrapeptides0 aStructural insights into the hydrogenbonding and folding pattern  cMAY  a2944–29493 aIn this paper, we provide structural insights into the hydrogen-bonding and folding pattern in Ant-Ant-Pro-Gly tetrapeptides (Ant: anthranilic acid; Pro: proline; and Gly: glycine). Comparison of the C-terminal esters and their amide analogs revealed strikingly different H-bonding networks. Whereas the ester analogs displayed an open structure without terminal H-bonding interactions, the amide analogs showed a completely folded structure. Structural details were revealed by using a combination of X-ray crystal structure studies and NOE-based molecular dynamics (MD) simulation studies.1 aBaravkar, Sachin, B.1 aKotmale, Amol, S.1 aMobin, Samir, R.1 aGonnade, Rajesh, Ghanshyam1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/structural-insights-hydrogen-bonding-and-folding-pattern-ant-ant-pro-gly-tetrapeptides