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Literature DB >> 7507751

Thermodynamics of BPTI folding.

G I Makhatadze¹, K S Kim, C Woodward, P L Privalov.

Abstract

A calorimetric study of the basic pancreatic trypsin inhibitor (BPTI) has been performed using the new generation of the adiabatic scanning microcalorimeters, operating in an extended temperature range of 5-130 degrees C. Precise measurements of the heat capacities of the native and unfolded states of BPTI show that the heat capacity change upon unfolding strongly depends on temperature; its value is maximal at about 50 degrees C and diminishes as the temperature is increased. The temperature dependencies of the enthalpy and entropy changes upon BPTI unfolding were found to be similar to those normally observed for other small globular proteins. The stability of BPTI has been correlated with its structure.

Entities: Disease

Mesh：

Substances：
Aprotinin

Year: 1993 PMID： 7507751 PMCID： PMC2142330 DOI： 10.1002/pro.5560021204

Source DB: PubMed Journal: Protein Sci ISSN： 0961-8368 Impact factor: 6.725

35 in total

1. The nature of the accessible and buried surfaces in proteins.

Authors: C Chothia
Journal: J Mol Biol Date: 1976-07-25 Impact factor: 5.469

2. Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects.

Authors: P L Privalov; G I Makhatadze
Journal: J Mol Biol Date: 1990-05-20 Impact factor: 5.469

3. The Protein Data Bank: a computer-based archival file for macromolecular structures.

Authors: F C Bernstein; T F Koetzle; G J Williams; E F Meyer; M D Brice; J R Rodgers; O Kennard; T Shimanouchi; M Tasumi
Journal: J Mol Biol Date: 1977-05-25 Impact factor: 5.469

4. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect.

Authors: G I Makhatadze; P L Privalov
Journal: J Mol Biol Date: 1990-05-20 Impact factor: 5.469

5. Reduced bovine pancreatic trypsin inhibitor has a compact structure.

Authors: D Amir; E Haas
Journal: Biochemistry Date: 1988-12-13 Impact factor: 3.162

6. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study.

Authors: P L Privalov; N N Khechinashvili
Journal: J Mol Biol Date: 1974-07-05 Impact factor: 5.469

7. Correction of light-scattering errors in spectrophotometric protein determinations.

Authors: A F Winder; W L Gent
Journal: Biopolymers Date: 1971 Impact factor: 2.505

Review 8. Stability of proteins: small globular proteins.

Authors: P L Privalov
Journal: Adv Protein Chem Date: 1979

9. Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains.

Authors: T C Wun; K K Kretzmer; T J Girard; J P Miletich; G J Broze
Journal: J Biol Chem Date: 1988-05-05 Impact factor: 5.157

10. The concentration dependence of the diffusion coefficient for bovine pancreatic trypsin inhibitor: a dynamic light scattering study of a small protein.

Authors: W H Gallagher; C K Woodward
Journal: Biopolymers Date: 1989-11 Impact factor: 2.505

22 in total

Thermodynamics of BPTI folding.

1. The nature of the accessible and buried surfaces in proteins.

2. Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects.

3. The Protein Data Bank: a computer-based archival file for macromolecular structures.

4. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect.

5. Reduced bovine pancreatic trypsin inhibitor has a compact structure.

6. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study.

7. Correction of light-scattering errors in spectrophotometric protein determinations.

Review 8. Stability of proteins: small globular proteins.

9. Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains.

10. The concentration dependence of the diffusion coefficient for bovine pancreatic trypsin inhibitor: a dynamic light scattering study of a small protein.

1. Are proteins well-packed?

2. The effect of net charge on the solubility, activity, and stability of ribonuclease Sa.

3. Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability.

4. Raman study of the thermal behaviour and conformational stability of basic pancreatic trypsin inhibitor.

5. Brownian dynamics simulation of protein solutions: structural and dynamical properties.

6. pH dependence thermal stability of a chymotrypsin inhibitor from Schizolobium parahyba seeds.

7. Biophysical characterization of a beta-peptide bundle: comparison to natural proteins.

8. Thermodynamics of the temperature-induced unfolding of globular proteins.

9. Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C.

10. Identification of cooperative folding units in a set of native proteins.