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Volumn 7, Issue 1, 1999, Pages 177-185

Optimization of hydrophobic domains in peptides that undergo transformation from α-Helix to β-fibril

Author keywords

helix; sheet; fibrillogenesis; Peptides and polypeptides; Structural transition

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DRUG DESIGN; HYDROPHOBICITY; IN VITRO STUDY; MOLECULAR DYNAMICS; PEPTIDE SYNTHESIS; PROTEIN DOMAIN; PROTEIN STRUCTURE;

EID: 0033015586     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(98)00236-3     Document Type: Article
Times cited : (51)

References (65)
  • 1
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    • Taubes, G. Science 1996, 271, 1492.
    • (1996) Science , vol.271 , pp. 1492
    • Taubes, G.1
  • 2
    • 0030572683 scopus 로고    scopus 로고
    • Wetzel, R. Cell 1996, 86, 699.
    • (1996) Cell , vol.86 , pp. 699
    • Wetzel, R.1
  • 44
    • 0344125381 scopus 로고    scopus 로고
    • note
    • In the previous studies, the concentration dependence of the transition of Ad-2α was investigated. Increases of peptide concentration of up to 10 μM linearly enhanced the reaction rate (slope) while shortening the lag time period for β-sheet formation. However, further increasing the concentration to more than 20 μM prevented the CD measurements due to the formation of insoluble materials. Under 10 μM concentration, no visible precipitate was observed. Thus, 10 μM concentration was selected as a standard condition.
  • 50
    • 0344556907 scopus 로고    scopus 로고
    • note
    • -1. According to this mechanism, the second self-catalytic step is 2000 times faster than the first non-catalytic step under the conditions ([peptide]=10 μM). This analysis suggests that the transitional reaction possibly proceeds via the first self-transitional and the second self-catalytic steps, in which there is a kinetic barrier at the first step. Although the aggregation numbers were not considered in this analysis, the first self-transitional step may include the aggregation of α-helix peptides. The temperature dependence of Ad-2α also suggested that the reaction occurring during the lag time was the rate-determining step and the rapid conformational transition followed.
  • 60
    • 0029820631 scopus 로고    scopus 로고
    • Mestel, R. Nature 1996, 273, 184.
    • (1996) Nature , vol.273 , pp. 184
    • Mestel, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.