Peptide-urea interactions as observed in diketopiperazine-urea cocrystal.
In order to develop a more complete understanding of urea induced protein denaturation we have investigated the crystal structure of urea with the cyclic dipeptide diketopiperazine. This structure, determined to an R factor of 8.1%, shows extensive hydrogen bonding between urea and the peptide groups of diketopiperazine. These studies support a model where hydrogen bonding plays an important contribution in urea-induced protein denaturation. In the companion paper we present thermodynamic data for urea-peptide interactions in aqueous solution that further support this model.
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.
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Thayer
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Haltiwanger
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Allured
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Gill
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Gill
D003460:Crystallization; D054659:Diketopiperazines; D004151:Dipeptides / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D010879:Piperazines / Q000737:chemistry*; D011489:Protein Denaturation; D014508:Urea / Q000737:chemistry*
D054659:Diketopiperazines; D004151:Dipeptides; D010879:Piperazines; D014508:Urea