메뉴 건너뛰기




Volumn 129, Issue 17, 2007, Pages 5308-5309

Environmental modulation of protein cation-π interactions

Author keywords

[No Author keywords available]

Indexed keywords

CATION;

EID: 34247853302     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja068957a     Document Type: Article
Times cited : (27)

References (21)
  • 20
    • 34247851545 scopus 로고    scopus 로고
    • Table 1 shows that the V32 proteins are more stable than those containing a Trp in position 32. The observed increase in stability most likely reflects a local structural relaxation occurring in the protein core upon changing W32 to a Val. The accuracy of the DMC analyses relies on the assumption that the energy associated with the W32 to V32 structural reorganization is uncoupled to the identity of the amino acid at position 36. That is, the 32 and 36 mutations are independent and protein reorganization terms will cancel in the DMC. 12 This assumption can be tested by comparing the difference in the W32/A36 and V32/A36 ΔG values (2.03 kcal/mol) to the difference in the W32/A36 and V32/K36 ΔG values after correcting for a Lys to Ala change in helical propensity (2.04 kcal/mol).14 Similar calculations for the R36 & H36 DMC analyses predict that the average discrepancy is in the order of 0.03 kcal mol-1. We conclude that the
    • -1. We conclude that the assumption made is valid.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.