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Persistent confusion on the van't Hoff equation.
- Published in:
- Biopolymers, 1997, v. 42, n. 5, p. 499, doi. 10.1002/(SICI)1097-0282(19971015)42:5<499::AID-BIP1>3.0.CO;2-L
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Erratum: 'the 'cratic correction' and related fallacies', vol. 35, no. 6, pp. 595-602 (1995).
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- Biopolymers, 1996, v. 39, n. 5, p. 753, doi. 10.1002/bip.360390503
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Tyrosines in two-stranded coiled coils are CD active near 280 nm even in the absence of interhelix tyrosine-tyrosine interactions.
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- Biopolymers, 1996, v. 38, n. 5, p. 669, doi. 10.1002/(SICI)1097-0282(199605)38:5<669::AID-BIP11>3.0.CO;2-3
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The use of spectral decomposition via the convex constraint algorithm in interpreting the CD-observed unfolding transitions of C coils.
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- Biopolymers, 1995, v. 36, n. 3, p. 365, doi. 10.1002/bip.360360310
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The 'cratic correction' and related fallacies.
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- Biopolymers, 1995, v. 35, n. 6, p. 595, doi. 10.1002/bip.360350605
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Some properties of acid-reassembled tropomyosin.
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- Biopolymers, 1995, v. 35, n. 2, p. 239, doi. 10.1002/bip.360350212
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Structural stability of short subsequences of the tropomyosin chain.
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- Biopolymers, 1995, v. 35, n. 1, p. 125, doi. 10.1002/bip.360350113
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Thermal unfolding equilibria in homodimeric chicken gizzard tropomyosin coiled coils.
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- Biopolymers, 1994, v. 34, n. 12, p. 1659, doi. 10.1002/bip.360341210
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Does Flory-Huggins theory help in interpreting solute partitioning experiments?
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- Biopolymers, 1994, v. 34, n. 3, p. 315, doi. 10.1002/bip.360340303
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Further characterization of the kinetic folding intermediate of αα-tropomyosin and of its 142-281 subsequence.
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- Biopolymers, 1993, v. 33, n. 5, p. 823, doi. 10.1002/bip.360330510
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α-helix to random coil transitions: Determination of peptide concentration from the CD at the isodichroic point.
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- Biopolymers, 1992, v. 32, n. 12, p. 1675, doi. 10.1002/bip.360321209
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α-Helix to random coil transitions: Interpretation of the CD in the region of linear temperature dependence.
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- Biopolymers, 1992, v. 32, n. 11, p. 1589, doi. 10.1002/bip.360321116
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Kinetics of folding and unfolding of ββ-tropomyosin.
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- Biopolymers, 1992, v. 32, n. 11, p. 1581, doi. 10.1002/bip.360321115
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The use of flory-huggins theory in interpreting partitioning of solutes between organic liquids and water.
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- Biopolymers, 1992, v. 32, n. 6, p. 711, doi. 10.1002/bip.360320611
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Kinetics of folding of αα-tropomyosin subsequences.
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- Biopolymers, 1992, v. 32, n. 7, p. 751, doi. 10.1002/bip.360320704
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Kinetics of folding and unfolding of αα-tropomyosin and of nonpolymerizable αα-tropomyosin.
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- Biopolymers, 1991, v. 31, n. 12, p. 1417, doi. 10.1002/bip.360311208
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The kinetics of chain exchange in two-chain coiled coils: αα- and ββ-tropomyosin.
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- Biopolymers, 1991, v. 31, n. 8, p. 957, doi. 10.1002/bip.360310805
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A scanning calorimetric study of the thermally induced unfolding of various forms of tropomyosin.
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- Biopolymers, 1991, v. 31, n. 5, p. 489, doi. 10.1002/bip.360310504
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α-Helix to random-coil transitions of two-chain coiled coils: The use of physical models in treating thermal denaturation equilibria of isolated subsequences of αα-tropomyosin.
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- Biopolymers, 1990, v. 30, n. 13/14, p. 1231, doi. 10.1002/bip.360301308
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The thermal denaturation of nonpolymerizable αα-tropomyosin and its segments as a function of ionic strength.
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- Biopolymers, 1990, v. 30, n. 9/10, p. 921, doi. 10.1002/bip.360300907
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α-Helix to random coil transitions of two-chain coiled coils: Experiments on the thermal denaturation of isolated segments of αα-tropomyosin.
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- Biopolymers, 1990, v. 30, n. 9/10, p. 985, doi. 10.1002/bip.360300913
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α-Helix to random coil transitions of two-chain coiled coils: Experiments on the thermal denaturation of ββ tropomyosin cross-linked selectively at C36.
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- Biopolymers, 1990, v. 29, n. 6/7, p. 1045, doi. 10.1002/bip.360290615
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The CD of two-chain coiled coils: Experiments on tropomyosin and tropomyosin segments in the tyrosin/disulfide spectral region.
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- Biopolymers, 1989, v. 28, n. 9, p. 1597, doi. 10.1002/bip.360280909
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The effect of sequence-specific interactions on the stability of the α-helix in synthetic tropomyosin-analogue peptides.
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- Biopolymers, 1989, v. 28, n. 4, p. 901, doi. 10.1002/bip.360280408
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α-Helix-to-random-coil transitions of two-chain coiled coils: Experiments on the thermal denaturation of ββ tropomyosin cross-linked selectively at C-190.
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- Biopolymers, 1988, v. 27, n. 8, p. 1223, doi. 10.1002/bip.360270804
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Application of the augmented theory of α-helix-to-random-coil transitions of two-chain, coiled coils to extant data on synthetic, tropomyosin-analog peptides.
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- Biopolymers, 1988, v. 27, n. 1, p. 87, doi. 10.1002/bip.360270107
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Hetero-α-helical, two-chain, coiled coils: αβ hybrid tropomysin.
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- Biopolymers, 1984, v. 23, n. 10, p. 1811, doi. 10.1002/bip.360231003
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Hetero-α-helical, two-chain coiled-coils. Clam-worm hybrid paramyosins.
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- Biopolymers, 1981, v. 20, n. 5, p. 925, doi. 10.1002/bip.1981.360200507
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Intrinsic viscosity of poly(α- L-glutamic acid) in N-methylacetamide.
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- Biopolymers, 1974, v. 13, n. 4, p. 853, doi. 10.1002/bip.1974.360130418
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On the use of the scheraga-mandelkern equation in determining molecular weights of very asymmetric proteins.
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- Biopolymers, 1963, v. 1, n. 5, p. 497, doi. 10.1002/bip.360010507
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Site-specific experiments on folding/unfolding of Jun coiled coils: Thermodynamic and kinetic parameters from spin inversion transfer nuclear magnetic resonance at leucine-18.
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- Biopolymers, 2006, v. 83, n. 3, p. 255, doi. 10.1002/bip.20555
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CD and <sup>13</sup>C<sup>α</sup>-NMR studies of folding equilibria in a two-stranded coiled coil formed by residues 190-254 of α-tropomyosin.
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- Biopolymers, 2001, v. 59, n. 4, p. 257, doi. 10.1002/1097-0282(20011005)59:4<257::AID-BIP1022>3.0.CO;2-7
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