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Volumn 126, Issue 3, 2004, Pages 790-796

Unexpectedly Fast Cis/Trans Isomerization of Xaa-Pro Peptide Bonds in Disulfide-Constrained Cyclic Peptides

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; CATALYSIS; HYDROGEN BONDS; ISOMERIZATION; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RATE CONSTANTS; STEREOCHEMISTRY; SULFUR COMPOUNDS; SYNTHESIS (CHEMICAL); THERMAL EFFECTS;

EID: 1642535352     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja030311k     Document Type: Article
Times cited : (50)

References (44)
  • 3
    • 0032486107 scopus 로고    scopus 로고
    • A specific peptide bond is generally conformationally homogeneous in the native, functional state of a protein. Forty-three percent of 617 protein structures from the Brookhaven protein database contain at least one Xaa-Pro peptide bond that is exclusively in the cis conformation in the native state. Reimer, U.; Scherer, G.; Drewello, M.; Kruber, S.; Schutkowski, M.; Fischer, G. J. Mol. Biol. 1998, 279, 449-460.
    • (1998) J. Mol. Biol. , vol.279 , pp. 449-460
    • Reimer, U.1    Scherer, G.2    Drewello, M.3    Kruber, S.4    Schutkowski, M.5    Fischer, G.6
  • 30
    • 1642489261 scopus 로고    scopus 로고
    • note
    • In most cases, the crude peptide obtained after cleavage contained more than 80% of the target dithiol peptide.
  • 38
    • 1642529873 scopus 로고    scopus 로고
    • note
    • TOCSY and ROESY spectra were measured at either 5 or 25 °C, as necessary to obtain resolved amide NH resonances.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.