Structural properties of an artificial protein that regulates the nucleation of inorganic and organic crystals

John L. Kulp, Tamiko Minamisawa, Kiyotaka Shiba, Margaret Tejani, John Evans

Research output: Contribution to journalArticle

Abstract

Technological advances have facilitated the generation of artificial proteins that possess the capabilities of recognizing and binding to inorganic solids and/or controlling nucleation processes that form inorganic solids. However, very little is known regarding the structure of these interesting polypeptides and how their structure contributes to functionality. To address this deficiency, we report structural investigations of an artificial protein, p288, that self-assembles and controls the nucleation of simple salts and organic compounds into dendrite-like crystals. Under aqueous conditions at low pH and in the presence of high salt, p288 is conformationally labile and exists primarily as a random coil conformer in equilibrium with other undefined secondary structures, including polyproline type II and β turn. We note that p288 can fold into either a partial β strand (at neutral pH) or a predominantly a helical (in the presence of TFE) conformation. Solid-state 13C-15N NMR experiments also reveal that p288 in the lyophilized, hydrated state possesses some degree of nonrandom coil structure. These results indicate that p288 is conformationally labile but can undergo conformational transitions to a more stable structure when water solvent loss/displacement occurs and protein concentrations increase. We believe that conformational instability and the ability to adopt different structures as a function of different environmental conditions represent important molecular features that impact p288 supramolecular assembly and crystal nucleation processes.

Original languageEnglish (US)
Pages (from-to)3857-3863
Number of pages7
JournalLangmuir
Volume23
Issue number7
DOIs
StatePublished - Mar 27 2007

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Structural properties
Nucleation
nucleation
proteins
Proteins
Crystals
coils
Salts
salts
crystals
Dendrites (metallography)
Polypeptides
polypeptides
Polytetrafluoroethylene
dendrites
organic compounds
Organic compounds
strands
Conformations
assembly

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Structural properties of an artificial protein that regulates the nucleation of inorganic and organic crystals. / Kulp, John L.; Minamisawa, Tamiko; Shiba, Kiyotaka; Tejani, Margaret; Evans, John.

In: Langmuir, Vol. 23, No. 7, 27.03.2007, p. 3857-3863.

Research output: Contribution to journalArticle

Kulp, John L. ; Minamisawa, Tamiko ; Shiba, Kiyotaka ; Tejani, Margaret ; Evans, John. / Structural properties of an artificial protein that regulates the nucleation of inorganic and organic crystals. In: Langmuir. 2007 ; Vol. 23, No. 7. pp. 3857-3863.
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