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3
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33745642314
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note
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i over a particular helical region equals the overall FH for that region.
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5
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0001887066
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The intrinsic tendency toward α-helix formation
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Vijayan, M., Yathindra, N., Kolaskar, A. S., Eds.; Indian Academy of Sciences: Bangalore
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For example: (a) Scheraga, H. A. The Intrinsic Tendency Toward α-Helix Formation. In Perspectives in Structural Biology; Vijayan, M., Yathindra, N., Kolaskar, A. S., Eds.; Indian Academy of Sciences: Bangalore, 1999; pp 275-282.
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Scheraga, H.A.1
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0030858237
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(c) Myers, J. K.; Pace, C. N.; Scholtz, J. M. Biochemistry 1997, 36, 10923-10929.
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Myers, J.K.1
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8
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33745673035
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In preparation
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Moreau, R. J.; Nasr, K. A.; Török, M.; Miller, J. S.; Schubert, C.; Kennedy, R. J.; Kemp, D. S. In preparation
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Moreau, R.J.1
Nasr, K.A.2
Török, M.3
Miller, J.S.4
Schubert, C.5
Kennedy, R.J.6
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(a) Miller, J. S.; Kennedy, R. J.; Kemp, D. S. Biochemistry 2001, 40, 305-309.
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0014243812
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(a) Ingwall, R. T. Scheraga, H. A.; Lotan, N.; Berger, A.; Katchalski, E. Biopolymers 1968, 6, 331-368.
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(c) Rothwarf, D. M.; Davenport, V. G.; Shi, P.-T.; Peng, J.-L.; Scheraga, H. A. Biopolymers 1996, 39, 531-536.
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(a) Heitmann, B.; Job, G. E.; Kennedy, R. J.; Walker, S. M.; Kemp, D. S. J. Am. Chem. Soc. 2005, 127, 1690-1704.
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(b) Job, G. E.; Heitmann, B.; Kennedy, R. J.; Walker, S. M.; Kemp, D. S. Angew. Chem., Int. Ed. 2004, 43, 5649-5651.
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16
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33745639072
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note
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2CO-) and beta ≡ β-amino-alanine.
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17
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(a) Chen, Y.-H.; Yang, J. T.; Martinez, H. M. Biochemistry 1972, 11, 4120-4131.
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nc, which has significant advantages: Kemp, D. S. Helv. Chim. Acta 2002, 85, 4392-4423.
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29
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33745647945
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note
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We employ a fixed ν = 0.048 to assign stabilities of single or paired residues with helical φ, Ψ angles, but to model helical end effects, we have replaced ν by t. A fixed w = 1.108 and a temperature-dependent t of 0.07 (a 45% increase from t = ν = 0.048 at 2 °C) successfully models Table 1 60 °C chemical shifts.
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30
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0025849701
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(a) Scholtz, J. M.; Marqusee, S.; Baldwin, R. L.; York, E. J.; Stewart, J. M.; Santoro, M.; Bolen, D. W. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 2854-2858.
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Marqusee, S.2
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Stewart, J.M.5
Santoro, M.6
Bolen, D.W.7
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(d) Richardson, J. M.; Lopez, M. M.; Makhatadze, G. L. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 1413-1418.
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Richardson, J.M.1
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Bai, Y.1
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Englander, S.W.4
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36
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33745661732
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note
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λ.U.T, see the Supporting Information.
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37
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0025752606
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Bruch, M. D.; Dhingra, M. M.; Gierasch, L. M. Proteins: Struct., Funct., Genet. 1991, 10, 130-139.
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40
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(b) Marshall, C. B.; Chakrabartty, A.; Davies, P. L. J. Biol. Chem. 2005, 280, 17920-17929.
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41
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33745664611
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note
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n peptides with n > 13 (temperature range 2-60 °C) showed double-slope 222 vs 208 nm parametric plots similar to that of Figure 6b. Three cases with n < 13 showed single-slope plots with slope ranges 2.2-2.3. A brief discussion of these, with an example, appears in the Supporting Information.
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42
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0016089450
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Gō, M.; Hesselink, F. T.; Gō, N.; Scheraga, H. Macromolecules 1974, 7, 459-467.
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Go, M.1
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Scheraga, H.4
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