2015
DOI: 10.1107/s205698901500393x
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Crystal structure of the tripeptideN-(benzyloxycarbonyl)glycylglycyl-L-norvaline

Abstract: The title tripeptide, C17H23N3O6, contains a nonproteinogenic C-terminal amino acid residue, norvaline, which is an isomer of the amino acid valine. Norvaline, unlike valine, has an unbranched side chain. The mol­ecule has a Gly–Gly segment which adopts an extended conformation. The norvaline residue also adopts an extended backbone conformation while its side chain has a g + t conformation. In the crystal lattice, N—H⋯O and O—H⋯O hydrogen bonds stabilize the packing. Mol­ecules translated along the crystallog… Show more

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Cited by 1 publication
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“…These special geometries are a parallel or antiparallel alignment between sidechain vectors and their orthogonal alignment with respect to backbone HB directions, as was pointed out previously in the study of the self-assembly of dipeptides [ 34 ]. Notably, both conformational states were found as the favorable assembly conformation for the multiple tripeptides was tested and agreed with the crystal structures of several others that had been reported previously [ 16 , 17 , 35 , 36 , 38 ], suggesting that they may be generic conformational features of tripeptides in fibrous assemblies. This finding could have an important implication in the design of assembling tripeptides: these conformations might serve as templates with which the design could begin, especially in a situation in which the design has to otherwise rely on either known experimental structures or a large number of conformational decoys, generated computationally [ 35 ].…”
Section: Discussionsupporting
confidence: 88%
“…These special geometries are a parallel or antiparallel alignment between sidechain vectors and their orthogonal alignment with respect to backbone HB directions, as was pointed out previously in the study of the self-assembly of dipeptides [ 34 ]. Notably, both conformational states were found as the favorable assembly conformation for the multiple tripeptides was tested and agreed with the crystal structures of several others that had been reported previously [ 16 , 17 , 35 , 36 , 38 ], suggesting that they may be generic conformational features of tripeptides in fibrous assemblies. This finding could have an important implication in the design of assembling tripeptides: these conformations might serve as templates with which the design could begin, especially in a situation in which the design has to otherwise rely on either known experimental structures or a large number of conformational decoys, generated computationally [ 35 ].…”
Section: Discussionsupporting
confidence: 88%