-
1
-
-
0033610474
-
Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation
-
Andersen NH, Dyer RB, Fesinmeyer RM, Gai F, Liu Z, Neidigh JW, Tong H. 1999. Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation. J Am Chem Soc 121:9878-9880.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 9878-9880
-
-
Andersen, N.H.1
Dyer, R.B.2
Fesinmeyer, R.M.3
Gai, F.4
Liu, Z.5
Neidigh, J.W.6
Tong, H.7
-
2
-
-
0000180763
-
Temperature dependence of the hydrophobic interaction in protein folding
-
Baldwin RL. 1986. Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA 83:8069-8072.
-
(1986)
Proc Natl Acad Sci USA
, vol.83
, pp. 8069-8072
-
-
Baldwin, R.L.1
-
3
-
-
6244250502
-
The role of hydrogen bonds in protein folding and protein association
-
Ben-Naim A. 1991. The role of hydrogen bonds in protein folding and protein association. J Phys Chem 95:1437-1444.
-
(1991)
J Phys Chem
, vol.95
, pp. 1437-1444
-
-
Ben-Naim, A.1
-
5
-
-
0014109212
-
Spectroscopic determination of tryptophan and tyrosine in proteins
-
Edelhoch H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
-
(1967)
Biochemistry
, vol.6
, pp. 1948-1954
-
-
Edelhoch, H.1
-
7
-
-
0031932824
-
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
-
Eliezer D, Yao J, Dyson HD, Wright PE. 1998. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat Struct Biol 5:148-155.
-
(1998)
Nat Struct Biol
, vol.5
, pp. 148-155
-
-
Eliezer, D.1
Yao, J.2
Dyson, H.D.3
Wright, P.E.4
-
8
-
-
0001022707
-
Protonation behavior of histidine 24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin
-
Geierstanger B, Jamin M, Volkman BF, Baldwin RL. 1998. Protonation behavior of histidine 24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin. Biochemistry 37:4254-4265.
-
(1998)
Biochemistry
, vol.37
, pp. 4254-4265
-
-
Geierstanger, B.1
Jamin, M.2
Volkman, B.F.3
Baldwin, R.L.4
-
9
-
-
3042788225
-
Calorimetric determination of enthalpies of solution of slightly soluble liquids. II. Enthalpy of solution of some hydrocarbons in water and their use in establishing the temperature dependence of their solubilities
-
Gill SJ, Nichols NF, Wadso I. 1976. Calorimetric determination of enthalpies of solution of slightly soluble liquids. II. Enthalpy of solution of some hydrocarbons in water and their use in establishing the temperature dependence of their solubilities. J Chem Thermodyn 8:445-452.
-
(1976)
J Chem Thermodyn
, vol.8
, pp. 445-452
-
-
Gill, S.J.1
Nichols, N.F.2
Wadso, I.3
-
10
-
-
0028174361
-
Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study
-
Griko YuV, Freire E, Privalov PL. 1994. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1899.
-
(1994)
Biochemistry
, vol.33
, pp. 1889-1899
-
-
Griko, Yu.V.1
Freire, E.2
Privalov, P.L.3
-
11
-
-
0028329347
-
Thermodynamic puzzle of apomyoglobin unfolding
-
Griko YuV, Privalov PL. 1994. Thermodynamic puzzle of apomyoglobin unfolding. J Mol Biol 235:1318-1325.
-
(1994)
J Mol Biol
, vol.235
, pp. 1318-1325
-
-
Griko, Yu.V.1
Privalov, P.L.2
-
13
-
-
0001220959
-
Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry
-
Hamada D, Fukada H, Takahashi K, Goto Y. 1995. Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry. Thermochim Acta 266:385-400.
-
(1995)
Thermochim Acta
, vol.266
, pp. 385-400
-
-
Hamada, D.1
Fukada, H.2
Takahashi, K.3
Goto, Y.4
-
14
-
-
0028143596
-
Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
-
Hamada D, Kidokoro S, Fukada H, Takahashi K, Goto Y. 1994. Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc Natl Acad Sci USA 91:10325-10329.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10325-10329
-
-
Hamada, D.1
Kidokoro, S.2
Fukada, H.3
Takahashi, K.4
Goto, Y.5
-
15
-
-
0027422525
-
Covalent bond changes as a driving force in enzyme catalysis
-
Huang Y, Bolen DW. 1993. Covalent bond changes as a driving force in enzyme catalysis. Biochemistry 32:9329-9339.
-
(1993)
Biochemistry
, vol.32
, pp. 9329-9339
-
-
Huang, Y.1
Bolen, D.W.2
-
16
-
-
0025186451
-
Structural characterization of a partly folded apomyoglobin intermediate
-
Hughson FM, Wright PE, Baldwin RL. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science 249:1544-1548.
-
(1990)
Science
, vol.249
, pp. 1544-1548
-
-
Hughson, F.M.1
Wright, P.E.2
Baldwin, R.L.3
-
17
-
-
0029904282
-
Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin
-
Jamin M, Baldwin RL. 1996. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin. Nat Struct Biol 3:613-618.
-
(1996)
Nat Struct Biol
, vol.3
, pp. 613-618
-
-
Jamin, M.1
Baldwin, R.L.2
-
18
-
-
0032549072
-
Two forms of the pH 4 folding intermediate of apomyoglobin
-
Jamin M, Baldwin RL. 1998. Two forms of the pH 4 folding intermediate of apomyoglobin. J Mol Biol 276:491-504.
-
(1998)
J Mol Biol
, vol.276
, pp. 491-504
-
-
Jamin, M.1
Baldwin, R.L.2
-
19
-
-
0033600716
-
Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate
-
Jamin M, Yen S-R, Rousseau DL, Baldwin RL. 1999. Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate. J Mol Biol 292:731-740.
-
(1999)
J Mol Biol
, vol.292
, pp. 731-740
-
-
Jamin, M.1
Yen, S.-R.2
Rousseau, D.L.3
Baldwin, R.L.4
-
20
-
-
0029981924
-
Packing interactions in the apomyoglobin folding intermediate
-
Kay MS, Baldwin RL. 1996. Packing interactions in the apomyoglobin folding intermediate. Nat Struct Biol 3:439-445.
-
(1996)
Nat Struct Biol
, vol.3
, pp. 439-445
-
-
Kay, M.S.1
Baldwin, R.L.2
-
21
-
-
0032568639
-
Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate
-
Kay MS, Baldwin RL. 1998. Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate. Biochemistry 37:7859-7868.
-
(1998)
Biochemistry
, vol.37
, pp. 7859-7868
-
-
Kay, M.S.1
Baldwin, R.L.2
-
22
-
-
0033514920
-
Specificity of native-like interhelical Hydrophobic contacts in the apomyoglobin intermediate
-
Kay MS, Ramos CHI, Baldwin RL. 1999. Specificity of native-like interhelical Hydrophobic contacts in the apomyoglobin intermediate. Proc Natl Acad Sci USA 96:2007-2012.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 2007-2012
-
-
Kay, M.S.1
Ramos, C.H.I.2
Baldwin, R.L.3
-
23
-
-
0015237085
-
On the nature of the protein interior
-
Klapper MH. 1971. On the nature of the protein interior. Biochim Biophys Acta 229:557-566.
-
(1971)
Biochim Biophys Acta
, vol.229
, pp. 557-566
-
-
Klapper, M.H.1
-
24
-
-
0029014386
-
Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
-
Loh SN, Kay MS, Baldwin RL. 1995. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc Natl Acad Sci USA 92:5446-5450.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 5446-5450
-
-
Loh, S.N.1
Kay, M.S.2
Baldwin, R.L.3
-
25
-
-
0033613115
-
The 28-111 disulfide bond constrains the a-lactalbumin molten globule and weakens its cooperativity of folding
-
Luo Y, Baldwin RL. 1999. The 28-111 disulfide bond constrains the a-lactalbumin molten globule and weakens its cooperativity of folding. Proc Natl Acad Sci USA 96:11283-11287.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 11283-11287
-
-
Luo, Y.1
Baldwin, R.L.2
-
26
-
-
0030694241
-
Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
-
Luo Y, Kay MS, Baldwin RL. 1997. Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations. Nat Struct Biol 4:925-930.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 925-930
-
-
Luo, Y.1
Kay, M.S.2
Baldwin, R.L.3
-
27
-
-
0027305948
-
Contribution of hydration to protein folding thermodynamics, 1. The enthalpy of hydration
-
Makhaladze GI, Privalov PL. 1993. Contribution of hydration to protein folding thermodynamics, 1. The enthalpy of hydration. J Mol Biol 232:639-659.
-
(1993)
J Mol Biol
, vol.232
, pp. 639-659
-
-
Makhaladze, G.I.1
Privalov, P.L.2
-
28
-
-
0029040449
-
Thermodynamic stability of the molten globule states of apomyoglobin
-
Nishii I, Kataoka M, Goto Y. 1995. Thermodynamic stability of the molten globule states of apomyoglobin. J Mol Biol 250:223-238.
-
(1995)
J Mol Biol
, vol.250
, pp. 223-238
-
-
Nishii, I.1
Kataoka, M.2
Goto, Y.3
-
29
-
-
0017429069
-
Areas, volumes, packing, and protein structure
-
Richards FM. 1977. Areas, volumes, packing, and protein structure. Ann Rev Biophys Bioeng 6:151-176.
-
(1977)
Ann Rev Biophys Bioeng
, vol.6
, pp. 151-176
-
-
Richards, F.M.1
-
30
-
-
0033613218
-
MEARA sequence of human CstF-64 polyadenylation factor is helical in solution. Aspectroscopic and calorimetric study
-
Richardson JM, McMahon KW, MacDonald CC, Makhatadze GI. 1999. MEARA sequence of human CstF-64 polyadenylation factor is helical in solution. Aspectroscopic and calorimetric study. Biochemistry 39:12869-12875.
-
(1999)
Biochemistry
, vol.39
, pp. 12869-12875
-
-
Richardson, J.M.1
McMahon, K.W.2
MacDonald, C.C.3
Makhatadze, G.I.4
-
31
-
-
49749194276
-
Studies on the structure of hemoglobin. 1. Physicochemical properties of human globin
-
Rossi-Fanelli A, Antonini E, Caputo A. 1958. Studies on the structure of hemoglobin. 1. Physicochemical properties of human globin. Biochim Biophys Acta 30:608-615.
-
(1958)
Biochim Biophys Acta
, vol.30
, pp. 608-615
-
-
Rossi-Fanelli, A.1
Antonini, E.2
Caputo, A.3
-
32
-
-
33947483983
-
Potentiometric titrations using Gran plots
-
Rossotti FJC, Rossotti H. 1965. Potentiometric titrations using Gran plots. J Chem Ed 42:375-378.
-
(1965)
J Chem Ed
, vol.42
, pp. 375-378
-
-
Rossotti, F.J.C.1
Rossotti, H.2
-
33
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
-
Santoro MM, Bolen DW. 1988, Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
34
-
-
0025849701
-
Calorimetric determination of the enthalpy change for the α-helix to coil transition of an alanine peptide in water
-
Scholtz JM, Marqusee S, Baldwin RL, York EJ, Stewart JM, Santoro MM, Bolen DW. 1991. Calorimetric determination of the enthalpy change for the α-helix to coil transition of an alanine peptide in water. Proc Natl Acad Sci USA 88:2854-2858.
-
(1991)
Proc Natl Acad Sci USA
, vol.88
, pp. 2854-2858
-
-
Scholtz, J.M.1
Marqusee, S.2
Baldwin, R.L.3
York, E.J.4
Stewart, J.M.5
Santoro, M.M.6
Bolen, D.W.7
-
35
-
-
0005123886
-
Thermodynamic properties of solutions of amino acids and related substances. VIII. The ionization of glycylglycine, ∈-aminocaproic acid, and aspartic acid in aqueous solution from one to fifty degrees
-
Smith ERB, Smith PK. 1942. Thermodynamic properties of solutions of amino acids and related substances. VIII. The ionization of glycylglycine, ∈-aminocaproic acid, and aspartic acid in aqueous solution from one to fifty degrees. J Biol Chem 146:187-195.
-
(1942)
J Biol Chem
, vol.146
, pp. 187-195
-
-
Smith, E.R.B.1
Smith, P.K.2
-
36
-
-
0033609809
-
A calorimetric study of an α-helix with covalently closed N and C-terminal loops
-
Taylor JW, Greenfield NJ, Wu B, Privalov PL. 1999. A calorimetric study of an α-helix with covalently closed N and C-terminal loops. J Mol Biol 291:965-476.
-
(1999)
J Mol Biol
, vol.291
, pp. 965-1476
-
-
Taylor, J.W.1
Greenfield, N.J.2
Wu, B.3
Privalov, P.L.4
-
37
-
-
0026800672
-
Analysis of the heat capacity dependence of protein folding
-
Yang A-S, Sharp KA, Honig B. 1992. Analysis of the heat capacity dependence of protein folding. J Mol Biol 227:889-900.
-
(1992)
J Mol Biol
, vol.227
, pp. 889-900
-
-
Yang, A.-S.1
Sharp, K.A.2
Honig, B.3
-
38
-
-
0028960492
-
How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
-
Yao M, Bolen DW. 1995. How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry 34:3771-3781.
-
(1995)
Biochemistry
, vol.34
, pp. 3771-3781
-
-
Yao, M.1
Bolen, D.W.2
-
39
-
-
0026679847
-
Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning calorimetry
-
Yutani K, Ogasahara K, Kuwajima K. 1992. Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning calorimetry. J Mol Biol 228:347-350.
-
(1992)
J Mol Biol
, vol.228
, pp. 347-350
-
-
Yutani, K.1
Ogasahara, K.2
Kuwajima, K.3
|