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Volumn 13, Issue 32, 2007, Pages 9004-9011

Coexistence of hydrogen-bonded loop and extended tetrapeptide conformations

Author keywords

Conformation analysis; Hydrogen bonds; NMR spectroscopy; Peptides; Photoisomerization

Indexed keywords

CONFORMATIONS; HYDROGEN BONDS; INFRARED SPECTROSCOPY; ISOTOPES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOTOISOMERIZATION;

EID: 36148969752     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200700396     Document Type: Article
Times cited : (10)

References (33)
  • 24
    • 36148929824 scopus 로고    scopus 로고
    • The factor by which the perpendicular signal was scaled in order to suppress the amide I diagonal signals in the difference spectra (factor used: 2.75) is not suitable for the ester band (factor: 2.64, As a result, in the weighted difference between the 2D-IR spectra recorded with parallel and perpendicular polarization the diagonal peak of the ester band is still weakly present. This difference (and the deviation from the theoretical scaling factor of 3) is tentatively assigned to faster fluctuations in the orientation of the ester C=O mode, which leads to a partial anisotropy decay before the probe pulse arrives 1 ps after the pump pulse
    • The factor by which the perpendicular signal was scaled in order to suppress the amide I diagonal signals in the difference spectra (factor used: 2.75) is not suitable for the ester band (factor: 2.64). As a result, in the weighted difference between the 2D-IR spectra recorded with parallel and perpendicular polarization the diagonal peak of the ester band is still weakly present. This difference (and the deviation from the theoretical scaling factor of 3) is tentatively assigned to faster fluctuations in the orientation of the ester C=O mode, which leads to a partial anisotropy decay before the probe pulse arrives 1 ps after the pump pulse.
  • 27
    • 36148993602 scopus 로고    scopus 로고
    • Another reason for the differences between the two tetrapeptides. in addition to that between crystal and solution structures, may be the conformation of the peptide bond between the Boc protection group and the first amino acid, which can adopt both the Z and the E forms. Crystalline Boc-L-phenylalanine, for example, is found in the E form, while the Z form typical of a regular peptide bond seems to dominate in solution (refs. [31, 32]).
    • Another reason for the differences between the two tetrapeptides. in addition to that between crystal and solution structures, may be the conformation of the peptide bond between the Boc protection group and the first amino acid, which can adopt both the Z and the E forms. Crystalline Boc-L-phenylalanine, for example, is found in the E form, while the Z form typical of a regular peptide bond seems to dominate in solution (refs. [31, 32]).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.