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Volumn 126, Issue 10, 2004, Pages 3261-3270

Investigation of Noncovalent Interactions in Deprotonated Peptides: Structural and Energetic Competition between Aggregation and Hydration

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CELLS; DIMERS; HYDRATION; MASS SPECTROMETERS; MOLECULAR DYNAMICS; PROBABILITY DENSITY FUNCTION;

EID: 1642367349     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0393628     Document Type: Article
Times cited : (48)

References (49)
  • 37
    • 1642364903 scopus 로고    scopus 로고
    • note
    • n+1 are very similar.
  • 44
    • 1642355164 scopus 로고    scopus 로고
    • note
    • The separated "frozen" structures are subjected to DFT minimization to obtain the structures shown in Figure 5b,d.
  • 47
    • 1642273782 scopus 로고    scopus 로고
    • note
    • 2O molecule to the deprotonated monomer. Entropy change scales with binding energy, and since the dialanine dimer is bound more than twice as strongly as each water of hydration, an entropy change 75% larger is not unreasonable. This magnitude of entropy change is also consistent with the much larger change in rotational entropy occurring on dimerization as compared to hydration, the dominate difference in the two processes.
  • 48
    • 1642348604 scopus 로고    scopus 로고
    • note
    • The term "hydrogen bond" is used here very loosely to describe any pairwise interaction between an electron-pair-accepting hydrogen atom and an electron-pair-donating atom without necessarily fulfilling the usual geometrical requirements (length ∼ 2 Å; angle ∼ 180°) used to define a hydrogen bond.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.