Long-range interactions stabilize the fold of a non-natural oligomer

Journal of the American Chemical Society

Volumn 124, Issue 39, 2002, Pages 11564-11565

  Cheng, Richard P ^a,b   DeGrado, William F ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

OLIGOMER; PROTEIN DERIVATIVE;

ARTICLE; CHEMICAL ANALYSIS; CHEMICAL INTERACTION; CHEMICAL STRUCTURE; PROTEIN FOLDING; PROTEIN STRUCTURE;

AMINOBUTYRIC ACIDS; CAPROATES; CIRCULAR DICHROISM; OLIGOPEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; VALERATES;

EID: 0037010015     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja020728a     Document Type: Article

References (23)

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23. Sedimentation equilibrium experiments were performed at 25 °C on samples in 10 mM PIPES buffer at pH 7.0 using a Beckman XL-I analytical ultrcentrifuge (loading concentrations between 0.1 and 0.4 mM). The samples were centrifuged for lengths of time sufficient to achieve equilibrium. Data obtained by UV absorption at 280 nm were analyzed by nonlinear least-squares fitting of radial concentration profiles using the Marquardt-Levenberg algorithm implemented in Igor Pro (Wave-metrics). Using the calculated partial specific volumes (0.787 and 0.777 mL/g for BHBmon and BHBox, respectively, from the method by Durchschlag, H.; Zipper, P. Prog. Colloid Polym. Sci. 1994, 94, 20-39), the data were fit to a single molecular weight species model. The resulting apparent molecular weights in solution for BHBmon and BHBox were 1984 and 3649 amu, respectively. For both cases, values within a±10% range of the apparent molecular weights gave reasonable fits and physical parameters. These values are consistent with the theoretical monomeric molecular weights for BHBmon (1745 amu) and BHBox (3695 amu).