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. Author manuscript; available in PMC: 2008 Sep 8.
Published in final edited form as: Biochemistry. 2005 Aug 30;44(34):11329–11341. doi: 10.1021/bi0501840

Table 2.

The dihedral angles (°) for calculated receptor bound conformations of fragments 2-12 of α-MSH and NDP-MSH.

Dihedral
angles
Residues
Tyr2 Ser3 Met4/
Nle4
Glu5 His6 LPhe7/
DPhe7
Arg8 Trp9 Gly10 Lys11 Pro12

α-MSH
ω 178 175 179 -176 171 -174 172 173 177 168 -179
φ -96 -170 -155 -83 -55 89 -67 -131 -163 -121 -74
ψ 106 105 159 -172 131 129 88 65 -144 78 127
Χ1 173 175 -34 -62 -76 -159 -63 -78 -174
Χ2 109 -145 81 -159 135 -67 130 -178
Χ3 -76 -92 143 -169
Χ4 -179 66

NDP-MSH
ω 178 169 -175 -170 174 178 177 169 173 176 -179
φ -174 -170 -155 -103 -73 157 60 -92 -162 -156 -63
ψ 125 114 153 -170 86 -22 52 88 -107 74 122
Χ1 -166 178 -73 -73 -80 159 -55 -60 -175
Χ2 80 -177 102 -114 99 -57 110 173
Χ3 -72 -63 177 -179
Χ4 121 70

α-MSH, Ac-Ser1-Tyr2-Ser3-Met4-Glu5-His6-Phe7-Arg8-Trp9-Gly10-Lys11-Pro12-Val13-NH2

NDP-MSH, [Nle4, -Phe7-]α-MSH