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Volumn 67, Issue 5 1, 2003, Pages

Role of bulk and of interface contacts in the behavior of lattice model dimeric proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHMS; AMINO ACIDS; COMPUTER SIMULATION; CONFORMATIONS; DIMERS; ENTROPY; GROUND STATE; INTERFACES (MATERIALS); LAGRANGE MULTIPLIERS; LATTICE CONSTANTS; MONTE CARLO METHODS; PHASE DIAGRAMS;

EID: 42749104264     PISSN: 1063651X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (4)

References (34)
  • 7
    • 33645074052 scopus 로고    scopus 로고
    • note
    • Because the bulk energy is always much larger than that associated with the interface, due to the fact that the number of native bulk contacts is much larger than the number of interface contacts, we shall refer, as a rule, to relative bulk and relative interface contact energies.
  • 15
    • 33645092285 scopus 로고    scopus 로고
    • note
    • The most ambitious classical molecular dynamics simulations have been able to study, starting from a random conformation, a small helix bundle [16] and to follow villin for about one-tenth of its folding time [17]. Making use of distributed computing implementation (a cluster of 30 000 volunteer computers around the world) a 23-residue protein has been followed from the denatured to the folded state [18].
  • 23
    • 33645075060 scopus 로고    scopus 로고
    • note
    • Whether the monomers are identical or related by mirror symmetry is immaterial within the framework of the minimal model of protein folding we employ.
  • 26
    • 33645092286 scopus 로고    scopus 로고
    • note
    • That is, low with respect to the only energy scale of the system, which is the standard deviation of the interaction matrix σ = 0.3.
  • 33
    • 33645070088 scopus 로고    scopus 로고
    • note
    • c = -48.3.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.