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Volumn 14, Issue 28, 2016, Pages 6780-6785

Replacing a single atom accelerates the folding of a protein and increases its thermostability

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CHAINS; FLUORINE; STABILITY;

EID: 84978859462     PISSN: 14770520     EISSN: None     Source Type: Journal    
DOI: 10.1039/c6ob00980h     Document Type: Article
Times cited : (21)

References (62)
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  • 20
    • 84978894739 scopus 로고    scopus 로고
    • Only 0.029% of non-prolyl peptide bonds are in the isomerization state in folded proteins. This prevalence increases to 5.21% for prolyl peptide bonds, which have nearly isoenergetic trans and cis isomers
    • Only 0.029% of non-prolyl peptide bonds are in the cis isomerization state in folded proteins. This prevalence increases to 5.21% for prolyl peptide bonds, which have nearly isoenergetic trans and cis isomers.
    • Cis
  • 30
    • 84978854612 scopus 로고    scopus 로고
    • W = 1.47 Å)
    • W = 1.47 Å)
  • 47
    • 0002846347 scopus 로고    scopus 로고
    • ed. T. E. Creighton, Oxford University Press, New York
    • C. N. Pace and J. M. Scholtz, in Protein Structure, ed., T. E. Creighton, Oxford University Press, New York, 1997, pp. 299-321
    • (1997) Protein Structure , pp. 299-321
    • Pace, C.N.1    Scholtz, J.M.2
  • 52
    • 84863490527 scopus 로고    scopus 로고
    • ed. E. C. Walters, Nova Science Publishers, New York, NY
    • U. Arnold, in Protein Folding, ed., E. C. Walters, Nova Science Publishers, New York, NY, 2011, pp. 83-118
    • (2011) Protein Folding , pp. 83-118
    • Arnold, U.1
  • 53
    • 0024279870 scopus 로고
    • D. J. Cram Science 1988 240 760 767
    • (1988) Science , vol.240 , pp. 760-767
    • Cram, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.