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Volumn 112, Issue 45, 2008, Pages 14302-14311

Relay stations for electron hole migration in peptides: Possibility for formation of three-electron bonds along peptide chains

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AROMATIC COMPOUNDS; CHEMICAL REACTIONS; DYNAMICS; ELECTRONS; MOLECULAR DYNAMICS; ORGANIC ACIDS; PEPTIDES; POLYPEPTIDES; PROTEINS; QUANTUM CHEMISTRY; SULFUR; TELECOMMUNICATION REPEATERS;

EID: 57049120519     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp805910x     Document Type: Article
Times cited : (28)

References (79)
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  • 8
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  • 47
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    • In this work, the amino acids will be represented by their three-letter abbreviations: Gly for glycine, Ala for alanine, Val for valine, Asp for asparagine, Cys for cysteine, Met for methionine, His for histidine, Phe for phenylalanine, Try for tyrosine, and Trp for tryptophan
    • In this work, the amino acids will be represented by their three-letter abbreviations: Gly for glycine, Ala for alanine, Val for valine, Asp for asparagine, Cys for cysteine, Met for methionine, His for histidine, Phe for phenylalanine, Try for tyrosine, and Trp for tryptophan.
  • 50
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    • (1996) Cerius2
  • 61
    • 84906406762 scopus 로고    scopus 로고
    • In native charge-transfer systems an electron is transported between donor and acceptor through large peptides and the electron migration is driven by electromotive potential between donor and acceptor. In this work, only the electron transfer bridges-polypeptide cations without additional donor and acceptor units attached were investigated and at 1000 K are to add a voltage (0.085 eV) in the systems ref 20
    • In native charge-transfer systems an electron is transported between donor and acceptor through large peptides and the electron migration is driven by electromotive potential between donor and acceptor. In this work, only the electron transfer bridges-polypeptide cations without additional donor and acceptor units attached were investigated and "at 1000 K" are to add a voltage (0.085 eV) in the systems (ref 20).
  • 62
    • 84906363751 scopus 로고    scopus 로고
    • 2 conformer can not come into being in all other dipeptide radical cation if there are no other stabilization factors, such as, hydrogen bonds and 3e bonds.
    • 2 conformer can not come into being in all other dipeptide radical cation if there are no other stabilization factors, such as, hydrogen bonds and 3e bonds.
  • 63
    • 84906406763 scopus 로고    scopus 로고
    • -O∴N is a bonding MO between these two close atoms. Therefore, there is a 2c-3e bond between the close O and N atoms arising from the interaction between the SOMO and the DOMO.
    • -O∴N is a bonding MO between these two close atoms. Therefore, there is a 2c-3e bond between the close O and N atoms arising from the interaction between the SOMO and the DOMO.
  • 64
    • 84906392010 scopus 로고    scopus 로고
    • ̇+-H and increases the stability.
    • ̇+-H and increases the stability.
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    • Neighboring group participation: General principles and application to sulfur-centered reactive species
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    • Glass, R. S. Neighboring group participation: General principles and application to sulfur-centered reactive species. In Sulfur-Centered Reactive Intermediates in Chemistry and Biology; Chatgilialoglu, C., Asmus, K.-D., Eds.; Plenum Press: New York, 1990; Vol. 97, pp 213-226.
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  • 75
    • 84906392011 scopus 로고    scopus 로고
    • It is well known that Trp and Tyr are easily oxidized in the processes of the protein redox reactions because both have the lowest ionization energies (IEs) among the natural a-amino acids. Their lowest IEs come from the special characters of their side chains, indole moiety in Trp and phenol moiety in Tyr. Our calculations indicate that the vertical IEs of 3-methylindole and 4-methylphenol are 7.40 and 7.96 eV, respectively, which agree well with previously results ref 65, For the side chains of His and Phe, the vertical IEs of 2-methylimidazole and toluene are 8.55 and 9.00 eV, respectively, which are bigger than these of 3-methylindole and 2-methylphenol
    • It is well known that Trp and Tyr are easily oxidized in the processes of the protein redox reactions because both have the lowest ionization energies (IEs) among the natural a-amino acids. Their lowest IEs come from the special characters of their side chains, indole moiety in Trp and phenol moiety in Tyr. Our calculations indicate that the vertical IEs of 3-methylindole and 4-methylphenol are 7.40 and 7.96 eV, respectively, which agree well with previously results (ref 65). For the side chains of His and Phe, the vertical IEs of 2-methylimidazole and toluene are 8.55 and 9.00 eV, respectively, which are bigger than these of 3-methylindole and 2-methylphenol.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.