메뉴 건너뛰기




Volumn 120, Issue 22, 1998, Pages 5568-5574

Barriers to rotation of secondary amide peptide bonds

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; AMPHOLYTE; AROMATIC AMINO ACID; IMIDE; OLIGOPEPTIDE; PENTAPEPTIDE; PHENYLALANINE; TYROSINE;

EID: 0032503605     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja980181t     Document Type: Article
Times cited : (158)

References (63)
  • 1
    • 33847490020 scopus 로고    scopus 로고
    • All amino acids are in the L configuration; NOESY, 2D nuclear Overhauser spectroscopy; MT, magnetization transfer
    • All amino acids are in the L configuration; NOESY, 2D nuclear Overhauser spectroscopy; MT, magnetization transfer.
  • 2
    • 33646964008 scopus 로고    scopus 로고
    • note
    • The term prolyl bond used throughout the paper indicates the peptide bond preceding proline in an amino acid sequence, and prolyl isomerization indicates the cis/trans isomerization of the peptide bond preceding proline. For secondary amide peptide bond isomerizations a similar nomenclature was used referring to tyrosyl isomerization when the cis isomerization of the secondary amide peptide bond preceding tyrosine was considered.
  • 14
    • 0001340839 scopus 로고
    • Creighton, T. E., Ed.; W. H. Freeman & Co.: New York
    • Schmid, F. X. In Protein Folding; Creighton, T. E., Ed.; W. H. Freeman & Co.: New York, 1992; pp 197-241.
    • (1992) Protein Folding , pp. 197-241
    • Schmid, F.X.1
  • 43
    • 33646956950 scopus 로고    scopus 로고
    • Marquardt, D. W. Share Distribution Center, 1964, program No. 1428
    • Marquardt, D. W. Share Distribution Center, 1964, program No. 1428.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.