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Refinado por: assunto: Calorimetric Enthalpy remover
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1
Spectroscopic and differential scanning calorimetric studies on the unfolding of Trichosanthes dioica seed lectin. Similar modes of thermal and chemical denaturation
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Spectroscopic and differential scanning calorimetric studies on the unfolding of Trichosanthes dioica seed lectin. Similar modes of thermal and chemical denaturation

Kavitha, M ; Swamy, Musti J

Glycoconjugate journal, 2009-11, Vol.26 (8), p.1075-1084 [Periódico revisado por pares]

Boston: Boston : Springer US

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2
Thermodynamics of the hydrophobic effect. I. Coupling of aggregation and pKa shifts in solutions of aliphatic amines
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Thermodynamics of the hydrophobic effect. I. Coupling of aggregation and pKa shifts in solutions of aliphatic amines

Matulis, Daumantas ; Bloomfield, Victor A.

Biophysical chemistry, 2001-10, Vol.93 (1), p.37-51 [Periódico revisado por pares]

Elsevier BV

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3
Significant discrepancies between van't Hoff and calorimetric enthalpies. III
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Significant discrepancies between van't Hoff and calorimetric enthalpies. III

Liu, Yufeng ; Sturtevant, Julian M.

Biophysical chemistry, 1997-02, Vol.64 (1), p.121-126 [Periódico revisado por pares]

Netherlands: Elsevier B.V

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4
Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines
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Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines

Matulis, Daumantas

Biophysical chemistry, 2001-10, Vol.93 (1), p.67-82 [Periódico revisado por pares]

Netherlands: Elsevier B.V

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5
Thermodynamics of the hydrophobic effect. II. Calorimetric measurement of enthalpy, entropy, and heat capacity of aggregation of alkylamines and long aliphatic chains
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Thermodynamics of the hydrophobic effect. II. Calorimetric measurement of enthalpy, entropy, and heat capacity of aggregation of alkylamines and long aliphatic chains

Matulis, Daumantas ; Bloomfield, Victor A.

Biophysical chemistry, 2001-10, Vol.93 (1), p.53-65 [Periódico revisado por pares]

Netherlands: Elsevier B.V

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6
Thermodynamics of the hydrophobic effect. I. Coupling of aggregation and p Ka shifts in solutions of aliphatic amines
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Thermodynamics of the hydrophobic effect. I. Coupling of aggregation and p Ka shifts in solutions of aliphatic amines

Matulis, Daumantas ; Bloomfield, Victor A.

Biophysical chemistry, 2001, Vol.93 (1), p.37-51 [Periódico revisado por pares]

Elsevier B.V

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7
Defining the Stability of Multimeric Proteins
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Defining the Stability of Multimeric Proteins

Shriver, John W. ; Edmondson, Stephen P.

Methods in molecular biology (Clifton, N.J.), 2009, Vol.490, p.57-82

Totowa, NJ: Humana Press

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