-
2
-
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0028209746
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Thermodynamic properties of peptide solutions. 11. Partial molar isentropic pressure coefficients in aqueous solutions of some tripeptides that model protein side-chains
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Hedwig GR, Høiland H. Thermodynamic properties of peptide solutions. 11. Partial molar isentropic pressure coefficients in aqueous solutions of some tripeptides that model protein side-chains. Biophys Chem. 49:1994;175-181.
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Hedwig, G.R.1
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3
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0000520789
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Partial molar isentropic pressure coefficients of some N-acetyl amino acid and peptide amides at infinite dilution in aqueous solutions at the temperature 298.15 K
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Hedwig GR, Høiland H. Partial molar isentropic pressure coefficients of some N-acetyl amino acid and peptide amides at infinite dilution in aqueous solutions at the temperature 298.15 K. J Chem Thermodyn. 27:1995;745-750.
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Hedwig, G.R.1
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4
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-
0030519064
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Thermodynamic properties of peptide solutions. 14. Partial molar expansibilities and isothermal compressibilities of some glycyl dipeptides in aqueous solutions
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Hedwig GR, Hastie JD, Høiland H. Thermodynamic properties of peptide solutions. 14. Partial molar expansibilities and isothermal compressibilities of some glycyl dipeptides in aqueous solutions. J Solut Chem. 25:1996;615-633.
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Hedwig, G.R.1
Hastie, J.D.2
Høiland, H.3
-
5
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-
0000673157
-
Thermodynamic properties of peptide solutions. 15. Partial molar isentropic compressibilities of some glycyl dipeptides in aqueous solutions at 15 and 36°C
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Hedwig GR, Høiland H, Hogseth E. Thermodynamic properties of peptide solutions. 15. Partial molar isentropic compressibilities of some glycyl dipeptides in aqueous solutions at 15 and 36°C. J Solut Chem. 25:1996;1041-1053.
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Hedwig, G.R.1
Høiland, H.2
Hogseth, E.3
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6
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0001514917
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Partial molar volumes, expansibilities, and compressibilities of α,ω-aminocarboxylic acids in aqueous solutions between 18 and 45°C
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Chalikian TV, Sarvazyan AP, Breslauer KJ. Partial molar volumes, expansibilities, and compressibilities of α,ω-aminocarboxylic acids in aqueous solutions between 18 and 45°C. J Phys Chem. 97:1993;13017-13026.
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Chalikian, T.V.1
Sarvazyan, A.P.2
Breslauer, K.J.3
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7
-
-
0028413422
-
Partial molar volumes, expansibilities, and compressibilities of oligoglycines in aqueous solutions at 18-55°C
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Chalikian TV, Sarvazyan AP, Funck T, Breslauer KJ. Partial molar volumes, expansibilities, and compressibilities of oligoglycines in aqueous solutions at 18-55°C. Biopolymers. 34:1994;541-553.
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Biopolymers
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Chalikian, T.V.1
Sarvazyan, A.P.2
Funck, T.3
Breslauer, K.J.4
-
8
-
-
0031709390
-
Hydration of diglycyl tripeptides with nonpolar side chain: A volumetric study
-
This paper reports the partial molar volumes and adiabatic compressibilities at 25°C of 10 X-Gly-Gly and Gly-Gly-X tripeptides in which X represents a residue with a nonpolar sidechain. The changes in volume and compressibility that accompany neutralization of the amino and carboxyl termini in these tripeptides also are reported. The authors interpret these results in terms of the hydration properties of the component aliphatic, aromatic and charged atomic groups, as well as in terms of the mutual interactions between these groups of special interest
-
Chalikian TV, Gindikin VS, Breslauer KJ. Hydration of diglycyl tripeptides with nonpolar side chain: a volumetric study. of special interest Biophys Chem. 75:1998; This paper reports the partial molar volumes and adiabatic compressibilities at 25°C of 10 X-Gly-Gly and Gly-Gly-X tripeptides in which X represents a residue with a nonpolar sidechain. The changes in volume and compressibility that accompany neutralization of the amino and carboxyl termini in these tripeptides also are reported. The authors interpret these results in terms of the hydration properties of the component aliphatic, aromatic and charged atomic groups, as well as in terms of the mutual interactions between these groups.
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(1998)
Biophys Chem
, vol.75
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Chalikian, T.V.1
Gindikin, V.S.2
Breslauer, K.J.3
-
9
-
-
0000765302
-
Partial molar characteristics of glycine and alanine in aqueous solutions at high pressures calculated from ultrasonic velocity data
-
Chalikian TV, Sarvazyan AP, Funck T, Cain CA, Breslauer KJ. Partial molar characteristics of glycine and alanine in aqueous solutions at high pressures calculated from ultrasonic velocity data. J Phys Chem. 98:1994;321-328.
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(1994)
J Phys Chem
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Chalikian, T.V.1
Sarvazyan, A.P.2
Funck, T.3
Cain, C.A.4
Breslauer, K.J.5
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10
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0025877453
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Protein hydration and function
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Rupley JA, Careri G. Protein hydration and function. Adv Protein Chem. 41:1991;37-172.
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Adv Protein Chem
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Rupley, J.A.1
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11
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-
0027993455
-
Hydration and partial compressibility of biological compounds
-
Chalikian TV, Sarvazyan AP, Breslauer KJ. Hydration and partial compressibility of biological compounds. Biophys Chem. 51:1994;89-109.
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(1994)
Biophys Chem
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, pp. 89-109
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Chalikian, T.V.1
Sarvazyan, A.P.2
Breslauer, K.J.3
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12
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-
0027535729
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Hydrational and intrinsic compressibilities of globular proteins
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Kharakoz DP, Sarvazyan AP. Hydrational and intrinsic compressibilities of globular proteins. Biopolymers. 33:1993;11-26.
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(1993)
Biopolymers
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Kharakoz, D.P.1
Sarvazyan, A.P.2
-
13
-
-
0030787855
-
Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure
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of special interest. The author uses an additivity approach to describe the hydration properties of globular proteins in their native, molten globule and unfolded states.
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Kharakoz DP. Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure. of special interest Biochemistry. 36:1997;10276-10285 The author uses an additivity approach to describe the hydration properties of globular proteins in their native, molten globule and unfolded states.
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(1997)
Biochemistry
, vol.36
, pp. 10276-10285
-
-
Kharakoz, D.P.1
-
14
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-
0008047756
-
The hydration of globular proteins as derived from volume and compressibility measurements: Cross correlating thermodynamic and structural data
-
Chalikian TV, Totrov M, Abagyan R, Breslauer KJ. The hydration of globular proteins as derived from volume and compressibility measurements: Cross correlating thermodynamic and structural data. J Mol Biol. 260:1996;588-603.
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(1996)
J Mol Biol
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, pp. 588-603
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Chalikian, T.V.1
Totrov, M.2
Abagyan, R.3
Breslauer, K.J.4
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15
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-
0029790358
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Packing at the protein - Water interface
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Gerstein M, Chothia C. Packing at the protein - water interface. Proc Natl Acad Sci USA. 93:1996;10167-10172.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 10167-10172
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Gerstein, M.1
Chothia, C.2
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16
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-
0030298077
-
On volume changes accompanying conformational transitions of biopolymers
-
Chalikian TV, Breslauer KJ. On volume changes accompanying conformational transitions of biopolymers. Biopolymers. 39:1996;619-626.
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(1996)
Biopolymers
, vol.39
, pp. 619-626
-
-
Chalikian, T.V.1
Breslauer, K.J.2
-
17
-
-
0032478214
-
Protein hydration in solution: Experimental observation by X-ray and neutron scattering
-
2O solutions. The results suggest the existence of a first hydration shell with an average density that is 10% larger than that of the bulk solvent.
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2O solutions. The results suggest the existence of a first hydration shell with an average density that is 10% larger than that of the bulk solvent.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 2267-2272
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-
Svergun, D.I.1
Richard, S.2
Koch, M.H.J.3
Sayers, Z.4
Kuprin, S.5
Zaccai, G.6
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18
-
-
0029859688
-
Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure
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Paci E, Marchi M. Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure. Proc Natl Acad Sci USA. 93:1996;11609-11614.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 11609-11614
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Paci, E.1
Marchi, M.2
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19
-
-
0031172372
-
On the volume of macromolecules
-
of special interest. The authors compare different definitions for the intrinsic volume of proteins. Particularly discussed are the molecular volume and the Voronoi volume. The authors emphasize that the Voronoi volume results in a better approximation of the experimental intrinsic compressibility.
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Paci E, Velikson B. On the volume of macromolecules. of special interest Biopolymers. 41:1997;785-797 The authors compare different definitions for the intrinsic volume of proteins. Particularly discussed are the molecular volume and the Voronoi volume. The authors emphasize that the Voronoi volume results in a better approximation of the experimental intrinsic compressibility.
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(1997)
Biopolymers
, vol.41
, pp. 785-797
-
-
Paci, E.1
Velikson, B.2
-
20
-
-
0001529341
-
Protein hydration and unfolding - Insights from experimental partial specific volumes and unfolded protein models
-
of outstanding interest. The authors seek to extract microscopic information about protein hydration and unfolding from experimental volumetric data using the idea that the protein - solvent interactions are proportional to the surface area of proteins. The authors discuss the effect of using different definitions of protein volume on the analysis of protein volumetric properties. The authors emphasize that the interpretation of hydration shell versus bulk water properties is model dependent.
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Murphy LR, Matubayasi N, Payne VA, Levy RM. Protein hydration and unfolding - insights from experimental partial specific volumes and unfolded protein models. of outstanding interest Fold Des. 3:1998;105-118 The authors seek to extract microscopic information about protein hydration and unfolding from experimental volumetric data using the idea that the protein - solvent interactions are proportional to the surface area of proteins. The authors discuss the effect of using different definitions of protein volume on the analysis of protein volumetric properties. The authors emphasize that the interpretation of hydration shell versus bulk water properties is model dependent.
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(1998)
Fold des
, vol.3
, pp. 105-118
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Murphy, L.R.1
Matubayasi, N.2
Payne, V.A.3
Levy, R.M.4
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21
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-
0344878444
-
Intrinsic volume and intrinsic compressibility of globular proteins
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Chalikian TV. Intrinsic volume and intrinsic compressibility of globular proteins. Biophys J. 74:1998;A273.
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(1998)
Biophys J
, vol.74
, pp. 273
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Chalikian, T.V.1
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22
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0000108733
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Compressibility of lysozyme protein crystals by X-ray diffraction
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Katrusiak A, Dauter Z. Compressibility of lysozyme protein crystals by X-ray diffraction. Acta Crystallogr. D52:1996;607-608.
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(1996)
Acta Crystallogr
, vol.52
, pp. 607-608
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-
Katrusiak, A.1
Dauter, Z.2
-
24
-
-
0031554921
-
Pressure-induced changes in the folded structure of lysozyme
-
of special interest. NMR measurements reveal pressure-induced changes in the overall folded structure of lysozyme. The authors suggest that the main effect of the pressure is a compaction of the hydrophobic core of the protein, which consists of bulky side chains.
-
Akasaka K, Tezuka T, Yamada H. Pressure-induced changes in the folded structure of lysozyme. of special interest J Mol Biol. 271:1997;671-678 NMR measurements reveal pressure-induced changes in the overall folded structure of lysozyme. The authors suggest that the main effect of the pressure is a compaction of the hydrophobic core of the protein, which consists of bulky side chains.
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(1997)
J Mol Biol
, vol.271
, pp. 671-678
-
-
Akasaka, K.1
Tezuka, T.2
Yamada, H.3
-
25
-
-
0032477750
-
Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor
-
1H NMR measurements under elevated pressures reveal that the signals of the peptide NH protons of basic pancreatic trypsin inhibitor (BPTI) in the folded state linearly shift their positions with pressure. Using these data, the authors estimate shortening of individual hydrogen bond distances at 2000 bar based on an the empirical shift-distance correlation for BPTI.
-
1H NMR measurements under elevated pressures reveal that the signals of the peptide NH protons of basic pancreatic trypsin inhibitor (BPTI) in the folded state linearly shift their positions with pressure. Using these data, the authors estimate shortening of individual hydrogen bond distances at 2000 bar based on an the empirical shift-distance correlation for BPTI.
-
(1998)
Biochemistry
, vol.37
, pp. 1167-1173
-
-
Li, H.1
Yamada, H.2
Akasaka, K.3
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26
-
-
0030028764
-
Glycerol decreases the volume and compressibility of protein interior
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Priev A, Almagor A, Yedgar S, Gavish B. Glycerol decreases the volume and compressibility of protein interior. Biochemistry. 35:1996;2061-2066.
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(1996)
Biochemistry
, vol.35
, pp. 2061-2066
-
-
Priev, A.1
Almagor, A.2
Yedgar, S.3
Gavish, B.4
-
27
-
-
0029971560
-
A large compressibility change of protein induced by a single amino acid substitution
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Gekko K, Tamura Y, Ohmae E, Hayashi H, Kagamiyama H, Ueno H. A large compressibility change of protein induced by a single amino acid substitution. Protein Sci. 5:1996;542-545.
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(1996)
Protein Sci
, vol.5
, pp. 542-545
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Gekko, K.1
Tamura, Y.2
Ohmae, E.3
Hayashi, H.4
Kagamiyama, H.5
Ueno, H.6
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28
-
-
0029157429
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Compact intermediate states in protein folding
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Fink AL. Compact intermediate states in protein folding. Annu Rev Biophys Biomol Struct. 24:1995;495-522.
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(1995)
Annu Rev Biophys Biomol Struct
, vol.24
, pp. 495-522
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Fink, A.L.1
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29
-
-
0031963564
-
Is the molten globule a third thermodynamic state of proteins? The example of α-lactalbumin
-
of special interest. Heat and denaturant-induced unfolding transitions of the molten globule state of α-lactalbumin are analyzed using calorimetric, viscometric and spectroscopic techniques. The author concludes that his results do not support the idea that the molten globule is a thermodynamic state.
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Pfeil W. Is the molten globule a third thermodynamic state of proteins? The example of α-lactalbumin. of special interest Proteins. 30:1998;43-48 Heat and denaturant-induced unfolding transitions of the molten globule state of α-lactalbumin are analyzed using calorimetric, viscometric and spectroscopic techniques. The author concludes that his results do not support the idea that the molten globule is a thermodynamic state.
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(1998)
Proteins
, vol.30
, pp. 43-48
-
-
Pfeil, W.1
-
30
-
-
0032539684
-
Is the molten globule a third phase of proteins?
-
of special interest. Using Monte Carlo simulations of two simplified models of protein-like heteropolymers, the authors obtain a generic phase diagram that contains a thermodynamically distinct molten globule state, in addition to the native and unfolded states.
-
Pande VS, Rokshar DS. Is the molten globule a third phase of proteins? of special interest Proc Natl Acad Sci USA. 95:1998;1490-1494 Using Monte Carlo simulations of two simplified models of protein-like heteropolymers, the authors obtain a generic phase diagram that contains a thermodynamically distinct molten globule state, in addition to the native and unfolded states.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 1490-1494
-
-
Pande, V.S.1
Rokshar, D.S.2
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31
-
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0029149109
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Application of pressure to biochemical equilibria: The other thermodynamic variable
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Royer CA. Application of pressure to biochemical equilibria: the other thermodynamic variable. Methods Enzymol. 259:1995;357-377.
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(1995)
Methods Enzymol
, vol.259
, pp. 357-377
-
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Royer, C.A.1
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32
-
-
0001746097
-
Pressure versus temperature behaviour of proteins
-
of outstanding interest. The authors critically analyze the results of recent studies on the effect of pressure on the structure and dynamics of proteins in the framework of the pressure - temperature stability phase diagram. It is suggested that pressure and temperature effects on proteins can be divided into elastic and conformational components. In this context, the authors discuss thermodynamic and kinetic aspects of protein unfolding in terms of hydration, intramolecular cavities and changes in secondary and tertiary structure.
-
Heremans K, Smeller L. Pressure versus temperature behaviour of proteins. of outstanding interest Eur J Solid State Inorg Chem. 34:1997;745-758 The authors critically analyze the results of recent studies on the effect of pressure on the structure and dynamics of proteins in the framework of the pressure - temperature stability phase diagram. It is suggested that pressure and temperature effects on proteins can be divided into elastic and conformational components. In this context, the authors discuss thermodynamic and kinetic aspects of protein unfolding in terms of hydration, intramolecular cavities and changes in secondary and tertiary structure.
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(1997)
Eur J Solid State Inorg Chem
, vol.34
, pp. 745-758
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-
Heremans, K.1
Smeller, L.2
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33
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12044253977
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The acidic molten globule state of α-lactalbumin probed by sound velocity
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Nölting B, Jiang M, Sligar SG. The acidic molten globule state of α-lactalbumin probed by sound velocity. J Am Chem Soc. 115:1993;9879-9882.
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(1993)
J Am Chem Soc
, vol.115
, pp. 9879-9882
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-
Nölting, B.1
Jiang, M.2
Sligar, S.G.3
-
34
-
-
0031019791
-
Molten globule of human α-lactalbumin: Hydration, density and compressibility of the interior
-
of special interest. Based on densimetric, ultrasonic velocimetric and sound absorption measurements, the authors conclude that the interior of the molten globule state of α-lactalbumin is accessible to water.
-
Kharakoz DP, Bychkova VE. Molten globule of human α-lactalbumin: hydration, density and compressibility of the interior. of special interest Biochemistry. 36:1997;1882-1890 Based on densimetric, ultrasonic velocimetric and sound absorption measurements, the authors conclude that the interior of the molten globule state of α-lactalbumin is accessible to water.
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(1997)
Biochemistry
, vol.36
, pp. 1882-1890
-
-
Kharakoz, D.P.1
Bychkova, V.E.2
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35
-
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0027373133
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Adiabatic compressibility of molten globules
-
Nölting B, Sligar SG. Adiabatic compressibility of molten globules. Biochemistry. 32:1993;12319-12323.
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(1993)
Biochemistry
, vol.32
, pp. 12319-12323
-
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Nölting, B.1
Sligar, S.G.2
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36
-
-
0029070645
-
Volume changes of the molten globule transitions of horse heart ferricytochrome c: A thermodynamic cycle
-
Foygel K, Spector S, Chatterjee S, Kahn PC. Volume changes of the molten globule transitions of horse heart ferricytochrome c: a thermodynamic cycle. Protein Sci. 4:1995;1426-1429.
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(1995)
Protein Sci
, vol.4
, pp. 1426-1429
-
-
Foygel, K.1
Spector, S.2
Chatterjee, S.3
Kahn, P.C.4
-
37
-
-
0029011017
-
Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH
-
Chalikian TV, Gindikin VS, Breslauer KJ. Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH. J Mol Biol. 250:1995;291-306.
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(1995)
J Mol Biol
, vol.250
, pp. 291-306
-
-
Chalikian, T.V.1
Gindikin, V.S.2
Breslauer, K.J.3
-
38
-
-
0028925816
-
Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
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Tamura Y, Gekko K. Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility. Biochemistry. 34:1995;1878-1884.
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(1995)
Biochemistry
, vol.34
, pp. 1878-1884
-
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Tamura, Y.1
Gekko, K.2
-
39
-
-
0343247668
-
The native and the heat-induced denatured states of α-chymotrypsinogen A: Thermodynamic and spectroscopic studies
-
of outstanding interest. A combination of densimetric, ultrasonic velocimetric, calorimetric and spectroscopic techniques are used to detect and characterize conformational transitions of α-chymotrypsinogen A as a function of both pH and temperature. The authors find that the heat-induced denatured state of the protein is unfolded at neutral and alkaline pH, while being molten globule-like at acidic pH. The results are interpreted in terms of hydration and intrinsic properties of the native, molten globule and unfolded states of α-chymotrypsinogen A.
-
Chalikian TV, Völker J, Anafi D, Breslauer KJ. The native and the heat-induced denatured states of α-chymotrypsinogen A: thermodynamic and spectroscopic studies. of outstanding interest J Mol Biol. 274:1997;237-252 A combination of densimetric, ultrasonic velocimetric, calorimetric and spectroscopic techniques are used to detect and characterize conformational transitions of α-chymotrypsinogen A as a function of both pH and temperature. The authors find that the heat-induced denatured state of the protein is unfolded at neutral and alkaline pH, while being molten globule-like at acidic pH. The results are interpreted in terms of hydration and intrinsic properties of the native, molten globule and unfolded states of α-chymotrypsinogen A.
-
(1997)
J Mol Biol
, vol.274
, pp. 237-252
-
-
Chalikian, T.V.1
Völker, J.2
Anafi, D.3
Breslauer, K.J.4
-
40
-
-
21944444619
-
Compressibility and volume changes of lysozyme due to guanidine hydrochloride denaturation
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Kamiyama T, Gekko K. Compressibility and volume changes of lysozyme due to guanidine hydrochloride denaturation. Chem Lett. 1997;1063-1064.
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(1997)
Chem Lett
, pp. 1063-1064
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Kamiyama, T.1
Gekko, K.2
-
41
-
-
0030059691
-
Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: Characterization of the base-induced unfolded state at 25°C
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Chalikian TV, Gindikin VS, Breslauer KJ. Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: characterization of the base-induced unfolded state at 25°C. FASEB J. 10:1996;164-170.
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(1996)
FASEB J
, vol.10
, pp. 164-170
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-
Chalikian, T.V.1
Gindikin, V.S.2
Breslauer, K.J.3
-
42
-
-
0030034601
-
Compressibility as a means to detect and characterize globular protein states
-
of outstanding interest. The authors report compressibility data on single domain, globular proteins that suggest a general relationship between protein conformational transitions and the change in the partial specific adiabatic compressibility that accompanies the transition. For single-domain globular proteins, the authors find that changes in the partial specific adiabatic compressibility correlate with the type of transition being monitored, independent of the specific protein.
-
Chalikian TV, Breslauer KJ. Compressibility as a means to detect and characterize globular protein states. of outstanding interest Proc Natl Acad Sci USA. 93:1996;1012-1014 The authors report compressibility data on single domain, globular proteins that suggest a general relationship between protein conformational transitions and the change in the partial specific adiabatic compressibility that accompanies the transition. For single-domain globular proteins, the authors find that changes in the partial specific adiabatic compressibility correlate with the type of transition being monitored, independent of the specific protein.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 1012-1014
-
-
Chalikian, T.V.1
Breslauer, K.J.2
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43
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0029143128
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Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR
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Yamaguchi T, Yamada H, Akasaka K. Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR. J Mol Biol. 250:1995;689-694.
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(1995)
J Mol Biol
, vol.250
, pp. 689-694
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-
Yamaguchi, T.1
Yamada, H.2
Akasaka, K.3
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44
-
-
0029737544
-
Testing the correlation between Δa and Δv of protein unfolding using m value mutants of staphylococcal nuclease
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Frye KJ, Perman CS, Royer CA. Testing the correlation between ΔA and ΔV of protein unfolding using m value mutants of staphylococcal nuclease. Biochemistry. 31:1996;10234-10239.
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(1996)
Biochemistry
, vol.31
, pp. 10234-10239
-
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Frye, K.J.1
Perman, C.S.2
Royer, C.A.3
-
45
-
-
0031837399
-
Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states
-
of special interest. The authors measure tryptophan emission spectra of apomyoglobin as a function of pressure. The resulting data are used to calculate the volume changes of the pressure-induced native-to-molten globule and molten globule-to-unfolded transitions. The authors conclude that the volume change associated with the hydration of protein surface upon unfolding may involve both positive and negative underlying contributions that effectively cancel. The authors also emphasize that the measured volume changes for protein conformational transitions arise from another source, perhaps, the elimination of void volume due to packing defects in the structured chains.
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Vidugiris GJA, Royer CA. Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states. of special interest Biophys J. 75:1998;463-470 The authors measure tryptophan emission spectra of apomyoglobin as a function of pressure. The resulting data are used to calculate the volume changes of the pressure-induced native-to-molten globule and molten globule-to-unfolded transitions. The authors conclude that the volume change associated with the hydration of protein surface upon unfolding may involve both positive and negative underlying contributions that effectively cancel. The authors also emphasize that the measured volume changes for protein conformational transitions arise from another source, perhaps, the elimination of void volume due to packing defects in the structured chains.
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Biophys J
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, pp. 463-470
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Vidugiris, G.J.A.1
Royer, C.A.2
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46
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0032574699
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Pressure denaturation of proteins: Evaluation of compressibility effects
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of outstanding interest. NMR measurements are employed to study pressure-induced denaturation of ribonuclease A. Based on a numerical analysis of the experimental results, the authors conclude that the compressibility difference between the native and pressure-induced unfolded species of the protein is a positive non-zero value. The authors emphasize that neglect of compressibility differences can skew the interpretation of experimental results.
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Prehoda KE, Mooberry ES, Markley JL. Pressure denaturation of proteins: evaluation of compressibility effects. of outstanding interest Biochemistry. 37:1998;5785-5790 NMR measurements are employed to study pressure-induced denaturation of ribonuclease A. Based on a numerical analysis of the experimental results, the authors conclude that the compressibility difference between the native and pressure-induced unfolded species of the protein is a positive non-zero value. The authors emphasize that neglect of compressibility differences can skew the interpretation of experimental results.
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(1998)
Biochemistry
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, pp. 5785-5790
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Prehoda, K.E.1
Mooberry, E.S.2
Markley, J.L.3
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47
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0028241354
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Hydration of DNA: Take 2
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Berman HM. Hydration of DNA: take 2. Curr Opin Struct Biol. 4:1994;345-350.
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Berman, H.M.1
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49
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0028222102
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Influence of base composition, base sequence, and duplex structure on DNA hydration: Apparent molar volumes and apparent molar adiabatic compressibilities of synthetic and natural DNA duplexes at 25°C
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Chalikian TV, Sarvazyan AP, Plum GE, Breslauer KJ. Influence of base composition, base sequence, and duplex structure on DNA hydration: apparent molar volumes and apparent molar adiabatic compressibilities of synthetic and natural DNA duplexes at 25°C. Biochemistry. 33:1994;2394-2401.
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Biochemistry
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Chalikian, T.V.1
Sarvazyan, A.P.2
Plum, G.E.3
Breslauer, K.J.4
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50
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0000877546
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Sequence dependent hydration of DNA: Theoretical results
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Elcock AH, MacCammon JA. Sequence dependent hydration of DNA: theoretical results. J Am Chem Soc. 117:1995;10161-10162.
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J Am Chem Soc
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Elcock, A.H.1
MacCammon, J.A.2
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51
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0027395923
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Volume changes correlate with entropies and enthalpies in the formation of nucleic acid homoduplexes: Differential hydration of A and B conformations
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Rentzeperis D, Kupke DW, Marky LA. Volume changes correlate with entropies and enthalpies in the formation of nucleic acid homoduplexes: differential hydration of A and B conformations. Biopolymers. 33:1993;117-125.
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Biopolymers
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Rentzeperis, D.1
Kupke, D.W.2
Marky, L.A.3
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52
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0027421534
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Pressure dependence of the melting temperature of dA·dT polymers
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Wu JQ, Macgregor RB Jr. Pressure dependence of the melting temperature of dA·dT polymers. Biochemistry. 32:1993;12531-12537.
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Biochemistry
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Wu, J.Q.1
MacGregor R.B., Jr.2
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53
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0028921926
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Pressure dependence of the helix-coil transition temperature of poly[d(GC)]
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Wu JQ, Macgregor RB Jr. Pressure dependence of the helix-coil transition temperature of poly[d(GC)]. Biopolymers. 35:1994;369-376.
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Biopolymers
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Wu, J.Q.1
MacGregor R.B., Jr.2
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54
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0028989686
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Effect of cations on the volume of the helix-coil transition of poly[d(AT)]
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Najaf-Zadeh R, Wu JQ, Macgregor RB Jr. Effect of cations on the volume of the helix-coil transition of poly[d(AT)]. Biochim Biophys Acta. 1262:1995;52-58.
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Najaf-Zadeh, R.1
Wu, J.Q.2
MacGregor R.B., Jr.3
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55
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0030026852
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Chain length and oligonucleotide stability at high pressure
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Macgregor RB Jr. Chain length and oligonucleotide stability at high pressure. Biopolymers. 38:1995;321-327.
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Biopolymers
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MacGregor R.B., Jr.1
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56
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0029811092
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The activation volume of a DNA helix-coil transition
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Lin M-C, Macgregor RB Jr. The activation volume of a DNA helix-coil transition. Biochemistry. 35:1996;11846-11851.
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Biochemistry
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Lin M-C1
MacGregor R.B., Jr.2
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57
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0030915958
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Activation volume of DNA duplex formation
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of outstanding interest. The authors use the pressure dependence of the denaturation-renaturation thermal hysteresis to investigate the kinetics of the helix-coil transitions of four 22-mer homopurine-homopyrimidine oligonucleotide duplexes with GC contents between 0.14 and 0.5. The data are interpreted in terms of the GC-dependence of the rate constants, activation volumes and volume changes that accompany helix formation.
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Lin M-C, Macgregor RB Jr. Activation volume of DNA duplex formation. of outstanding interest Biochemistry. 36:1997;6539-6544 The authors use the pressure dependence of the denaturation-renaturation thermal hysteresis to investigate the kinetics of the helix-coil transitions of four 22-mer homopurine-homopyrimidine oligonucleotide duplexes with GC contents between 0.14 and 0.5. The data are interpreted in terms of the GC-dependence of the rate constants, activation volumes and volume changes that accompany helix formation.
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Biochemistry
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Lin M-C1
MacGregor R.B., Jr.2
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58
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0028142863
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The influence of drug binding on DNA hydration: Acoustic and densimetric characterizations of netropsin binding to the poly(dAdT)poly(dAdT) and the poly(dA)poly(dT) duplexes and to the poly(dT)poly(dA)poly(dT) triplex at 25°C
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Chalikian TV, Plum GE, Sarvazyan AP, Breslauer KJ. The influence of drug binding on DNA hydration: acoustic and densimetric characterizations of netropsin binding to the poly(dAdT)poly(dAdT) and the poly(dA)poly(dT) duplexes and to the poly(dT)poly(dA)poly(dT) triplex at 25°C. Biochemistry. 33:1994;8629-8640.
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Biochemistry
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Chalikian, T.V.1
Plum, G.E.2
Sarvazyan, A.P.3
Breslauer, K.J.4
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60
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0029763453
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Hydration effects accompanying the substitution of counterions in the ionic atmosphere of poly(rA)poly(rU) and poly(rA)2poly(rU) helices
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Buckin V, Tran H, Morozov V, Marky LA. Hydration effects accompanying the substitution of counterions in the ionic atmosphere of poly(rA)poly(rU) and poly(rA)2poly(rU) helices. J Am Chem Soc. 118:1996;7033-7039.
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Buckin, V.1
Tran, H.2
Morozov, V.3
Marky, L.A.4
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