Literature DB >> 9878408

Structural differences in D and L-monellin in the crystals of racemic mixture.

L W Hung1, M Kohmura, Y Ariyoshi, S H Kim.   

Abstract

The racemic mixture of synthetic d and l-monellin has been crystallized, and its structure has been determined by X-ray crystallography at 1.9 A resolution. The crystal structure consists of two d and two l-monellin molecules in the P1 unit cell with a pseudo-centrosymmetrical arrangement. The final structure reveals small but significant structural differences between d and l-monellin in the same crystal. Possible reasons for these differences and their implications are discussed. Copyright 1999 Academic Press.

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Year:  1999        PMID: 9878408     DOI: 10.1006/jmbi.1998.2308

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  15 in total

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4.  Quasiracemic crystallization as a tool to assess the accommodation of noncanonical residues in nativelike protein conformations.

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8.  X-ray structure of native scorpion toxin BmBKTx1 by racemic protein crystallography using direct methods.

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9.  Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods.

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Review 10.  Protein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structure.

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Journal:  Org Biomol Chem       Date:  2014-11-28       Impact factor: 3.876

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