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Volumn 119, Issue 36, 1997, Pages 8547-8561

Extracting information from the temperature gradients of polypeptide NH chemical shifts. 1. The importance of conformational averaging

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AMIDE;

EID: 0030858227     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja963250h     Document Type: Article
Times cited : (232)

References (121)
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    • note
    • Although a number of the authors used NH temperature gradients to confirm loci of structuring, our exclusions of NH points appearing in Figure 3 from the correlation shown in Table 2 were based only on NOE and scalar coupling observations.
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    • See, for examples ref 24 and (a) Shoemaker, K. R.; Kim, P. S.; Brems, D. N.; Marqusee, S.; York, E. J.; Chaiken, I. M.; Stewart, J. M.; Baldwin, R. L. Proc. Natl. Acad. Sci. U.S.A. 1985, 82, 2349-2353. (b) Osterhout, J. J., Jr.; Baldwin, R. L.; York, E. J.; Stewart, J. M.; Dyson, H. J.; Wright, P. E. Biochemistry 1989, 28, 7059-7064. (c) Dtrehlow, K. G.; Robertson, A. D.; Baldwin, R. L. Biochemistry 1991, 30, 5810-5814.
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    • in press
    • (b) For further details of the calculations used in this helix/coil model, see: Andersen, N. H.; Tong, H. Protein Sci. 1997, 6, in press.
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    • note
    • 12d Due to unfolding upon warming, such NHs would display a less negative Δδ/ΔT due to the increasing contribution of solvated species in the population weighted average at the higher temperature.


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