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Volumn 132, Issue 5, 2010, Pages 1621-1630

NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: Implications for oligomer formation by 3D domain swapping

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FORMATION; BIOCHEMICAL PROCESS; CONCENTRATED SOLUTION; DOMAIN SWAPPING; FOLDING KINETICS; GUANIDINIUM CHLORIDES; HETERONUCLEAR; MOLECULAR MECHANISM; MONOMERIC PROTEINS; N-TERMINALS; NMR SPECTROSCOPY; NON-NATIVE; PEPTIDE BONDS; REFOLDING; RIBONUCLEASE A; RNASE A; SELF-RECOGNITION; TRANS CONFORMATIONS; UV CIRCULAR DICHROISM;

EID: 76149127360     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9081638     Document Type: Article
Times cited : (61)

References (71)
  • 1
    • 0001005285 scopus 로고    scopus 로고
    • Raines, R. T. Chem. Rev. 1998, 98, 1045-1065.
    • (1998) Chem. Rev , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 30
    • 0004199373 scopus 로고    scopus 로고
    • Creighton, T. E, Ed, Oxford University Press: Oxford
    • Pace, C. N.; Scholtz, J. M. In Protein Structure; Creighton, T. E., Ed.; Oxford University Press: Oxford, 1997; pp 253-259.
    • (1997) Protein Structure , pp. 253-259
    • Pace, C.N.1    Scholtz, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.