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. Author manuscript; available in PMC: 2016 Oct 6.
Published in final edited form as: Biochemistry. 2015 Oct 6;54(39):6029–6037. doi: 10.1021/acs.biochem.5b00622

Figure 7.

Figure 7

Water distribution around the Gly substitution sites: (a) crystal structure18 and (b) MD solution from top view of the N terminal triple helix. In (a), W1 bridges the amide group of LA15 in the L chain and carbonyl group of Pro in the M chain. W2 and W3 are the water bridges of MA15 and TA15, respectively. W4 represents a water bridge for LG18. In (b), the MD simulated water density is shown with contour lines, which are coded by the total occupancy level of the volume. Volumes occupied > 75% are shown in red, > 50% in orange, and > 25% in blue. Crystal interstitial waters (W1–W3) are marked as red spheres; the three Ala are represented as licorice; Pro and Hyp are colored in orange and gray, respectively. Schematic of the hydrogen bonding topology around the Gly substitution sites (gray area) of a G→A peptide in the (c) crystal form and (d) solution form. Direct inter-chain hydrogen bonds are indicated as solid lines, hydrogen bonding to water is represented with the W label in the circle.