메뉴 건너뛰기




Volumn 71, Issue 18, 1999, Pages 3965-3973

Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; METHIONINE; OXYGEN 18; PHENYLALANINE; POLYPEPTIDE; PROLINE; TYROSINE;

EID: 0033568535     PISSN: 00032700     EISSN: None     Source Type: Journal    
DOI: 10.1021/ac990500e     Document Type: Article
Times cited : (203)

References (53)
  • 1
    • 0026795635 scopus 로고
    • (a) Stadtman, E. R. Science 1992, 257, 1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 32
    • 0345199440 scopus 로고    scopus 로고
    • note
    • The term "hydroxylation" refers to modifications of amino acids from reactions with hydroxyl radicals that originate from water (eq 1). The term "oxidation" is used for modifications induced by oxygen radical species derived from molecular oxygen (eq 2).
  • 42
    • 84987419408 scopus 로고
    • When the peptide bond cleaves at the amide bond and the charge is retained on the N-terminal portion, the fragment is referred to as b-type ion, and charge retention on the C-terminus yields y-type ion: (a) Roepstorff, P.; Fohlmann, J. Biomed. Mass Spectrum. 1984, 11, 601. (b) Biemann, K. Biomed. Environ. Mass Spectrom. 1988, 16, 99.
    • (1984) Biomed. Mass Spectrum. , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlmann, J.2
  • 43
    • 0023804303 scopus 로고
    • When the peptide bond cleaves at the amide bond and the charge is retained on the N-terminal portion, the fragment is referred to as b-type ion, and charge retention on the C-terminus yields y-type ion: (a) Roepstorff, P.; Fohlmann, J. Biomed. Mass Spectrum. 1984, 11, 601. (b) Biemann, K. Biomed. Environ. Mass Spectrom. 1988, 16, 99.
    • (1988) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 99
    • Biemann, K.1
  • 51
    • 0345199433 scopus 로고    scopus 로고
    • Solvent-accessible surface area maps of proteins are derived from crystal structures by utilizing a computer program, VADAR, Protein engineering network of Centers of Excellence, University of Alberta, Canada
    • Solvent-accessible surface area maps of proteins are derived from crystal structures by utilizing a computer program, VADAR, Protein engineering network of Centers of Excellence, University of Alberta, Canada.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.