Abstract
Insulin crystallizes in different forms, some of which show different conformations for the different molecules in the asymmetric unit. This observation leads to the question as to which conformation the molecule will adopt in solution. Molecular dynamics computer simulations of rhombohedral 2 Zn pig insulin have been carried out for both monomers (1 and 2) independently in order to study their behaviour in the absence of quaternary structure and crystal packing forces.
These preliminary 120 ps simulations suggest that both monomers converge in solution to very similar conformations which differ from the X-ray structures of both monomer 1 and 2 (Chinese nomenclature), but are closer to the former, as has previously been suggested by an analysis of the crystal packing (Chothia et al. 1983) and by energy minimization (Wodak et al. 1984). The secondary structure of the molecules is basically preserved, as expected. A detailed description of the conformational changes is given.
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Abbreviations
- MD:
-
Molecular dynamics (simulations)
- EM:
-
Energy minimization
- X1:
-
X-ray structure of molecule 1
- X2:
-
X-ray structure of molecule 2
- MD1:
-
mean simulated structure of molecule 1
- MD2:
-
mean simulated structure of molecule 2
- A N helix:
-
helix at the N-terminal part of the insulin A-chain
- A C helix:
-
helix at the C-terminal part of the insulin A-chain. One and three-letter abbreviations for amino acids are used.
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Krüger, P., Straßburger, W., Wollmer, A. et al. The simulated dynamics of the insulin monomer and their relationship to the molecule's structure. Eur Biophys J 14, 449–459 (1987). https://doi.org/10.1007/BF00293254
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DOI: https://doi.org/10.1007/BF00293254