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Volumn 32, Issue 1, 2004, Pages 31-34

A Spectroscopic-based Laboratory Experiment for Protein Conformational Studies

Author keywords

Circular dichroism; Fluorescence; Laboratory class; Protein folding and stability

Indexed keywords

ANALYTIC METHOD; ARTICLE; BIOCHEMISTRY; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; FLUORESCENCE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; SPECTROPHOTOMETRY; SPECTROSCOPY; TEACHING; TECHNIQUE;

EID: 1642576024     PISSN: 14708175     EISSN: None     Source Type: Journal    
DOI: 10.1002/bmb.2004.494032010309     Document Type: Article
Times cited : (23)

References (11)
  • 2
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    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 4
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • H. Edelhoch (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 5
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution I. Crystallographic refinement of metmyoglobin from sperm whale
    • T. Takano (1977) Structure of myoglobin refined at 2.0 Å resolution I. Crystallographic refinement of metmyoglobin from sperm whale. J. Mol. Biol. 110, 537-568.
    • (1977) J. Mol. Biol. , vol.110 , pp. 537-568
    • Takano, T.1
  • 6
    • 0023910427 scopus 로고
    • Horse heart metmyoglobin. A 2.8-A resolution three-dimensional structure determination
    • S. V. Evans, G. D. Brayer (1988) Horse heart metmyoglobin. A 2.8-A resolution three-dimensional structure determination. J. Biol. Chem. 263, 4263-4268.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4263-4268
    • Evans, S.V.1    Brayer, G.D.2
  • 8
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • M. R. Eftink. (1994) The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66, 482-501.
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 10
    • 0033609475 scopus 로고    scopus 로고
    • Putative ion pairs involved in myoglobin stability
    • C. H. I. Ramos, M. S., Kay, R. L. Baldwin (1999) Putative ion pairs involved in myoglobin stability, Biochemistry 38, 9783-9790.
    • (1999) Biochemistry , vol.38 , pp. 9783-9790
    • Ramos, C.H.I.1    Kay, M.S.2    Baldwin, R.L.3
  • 11
    • 0036081128 scopus 로고    scopus 로고
    • Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect
    • C. H. I. Ramos, R. L. Baldwin (2002) Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect. Protein Sci. 11, 1771-1778.
    • (2002) Protein Sci. , vol.11 , pp. 1771-1778
    • Ramos, C.H.I.1    Baldwin, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.