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Volumn 3, Issue 6, 1999, Pages 714-723

Designed molecules that fold to mimic protein secondary structures

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE;

EID: 0032705432     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)00030-7     Document Type: Review
Times cited : (233)

References (51)
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    • Ranganathan D., Haridas V., Kurur S., Thomas A., Madhusudanan K.P., Nagaraj R., Kunwar A.C., Sarma A.V.S., Karle I.L. Demonstration of endo-cis-(2S,3R)-bicyclo[2.2.1]hept-5-en-2,3-dicarbonyl unit as a reverse-turn scaffold and nucleator of two-stranded parallel β-sheets: design, synthesis, crystal structure, and self-assembling properties of norborneno peptide analogues. J Am Chem Soc. 120:1998;8448-8460.
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    • Molecular modeling, synthesis, and structures of N-methylated 3,5-linked pyrrolin-4-ones toward the creation of a privileged nonpeptide scaffold
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    • β-Turn and β-hairpin mimicry with tetrasubstituted alkenes
    • This paper contains a full study of the Gellman group's acyclic β-turn mimic reported in [39] and investigates the alternative conformations accessed by peptide strands containing this turn unit
    • Gardner R.R., Liang G.-B., Gellman S.H. β-Turn and β-hairpin mimicry with tetrasubstituted alkenes. J Am Chem Soc. 121:1999;1806-1816. This paper contains a full study of the Gellman group's acyclic β-turn mimic reported in [39] and investigates the alternative conformations accessed by peptide strands containing this turn unit.
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    • The authors describe a heterochiral nipecotic acid dimer that nucleates β-hairpin turns. Interestingly, the homochiral nipecotic dimer does not exhibit the internal hydrogen bonding required for a turn. In conjunction with previous studies, this study confirms that β-peptides can access all three protein secondary structures
    • Chung Y.J., Christianson L.A., Stanger H.E., Powell D.R., Gellman S.H. A β-peptide reverse turn that promotes hairpin formation. J Am Chem Soc. 120:1998;10555-10556. The authors describe a heterochiral nipecotic acid dimer that nucleates β-hairpin turns. Interestingly, the homochiral nipecotic dimer does not exhibit the internal hydrogen bonding required for a turn. In conjunction with previous studies, this study confirms that β-peptides can access all three protein secondary structures.
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    • Chung, Y.J.1    Christianson, L.A.2    Stanger, H.E.3    Powell, D.R.4    Gellman, S.H.5
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    • The authors describe the synthesis of a β-sheet mimic that dimerizes. This result suggests that similar compounds can be designed to interfere with the β-sheets formed at protein-protein interfaces
    • Nowick J.S., Tsai J.H., Bui Q.-C.D., Maitra S. A chemical model of a protein β-sheet dimer. J Am Chem Soc. 121:1999;8409-8410. The authors describe the synthesis of a β-sheet mimic that dimerizes. This result suggests that similar compounds can be designed to interfere with the β-sheets formed at protein-protein interfaces.
    • (1999) J Am Chem Soc , vol.121 , pp. 8409-8410
    • Nowick, J.S.1    Tsai, J.H.2    Bui, Q.-C.D.3    Maitra, S.4
  • 50
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    • A new approach for the design of supramolecular recognition units: Hydrogen-bonded molecular duplexes
    • Gong B., Yan Y., Zeng H., Skrzypczak-Jankunn E., Kim Y.W., Zhu J., Ickes H. A new approach for the design of supramolecular recognition units: hydrogen-bonded molecular duplexes. J Am Chem Soc. 121:1999;3007-3008.
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    • Gong, B.1    Yan, Y.2    Zeng, H.3    Skrzypczak-Jankunn, E.4    Kim, Y.W.5    Zhu, J.6    Ickes, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.