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Literature DB >> 469937

Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor.

G Wagner, K Wüthrich.

Abstract

Entities: Chemical Disease Gene

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Year: 1979 PMID： 469937 DOI： 10.1016/0022-2836(79)90550-3

Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469

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19 in total

1. Nativelike enzyme properties are important for optimum activity in neat organic solvents.

Authors: K Griebenow; M Vidal; C Baéz; A M Santos; G Barletta
Journal: J Am Chem Soc Date: 2001-06-06 Impact factor: 15.419

2. Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase.

Authors: J Fitter; J Heberle
Journal: Biophys J Date: 2000-09 Impact factor: 4.033

3. NMR solution structure of the activation domain of human procarboxypeptidase A2.

Authors: M Angeles Jiménez; Virtudes Villegas; Jorge Santoro; Luis Serrano; Josep Vendrell; Francesc X Avilés; Manuel Rico
Journal: Protein Sci Date: 2003-02 Impact factor: 6.725

4. Neutralizing positive charges at the surface of a protein lowers its rate of amide hydrogen exchange without altering its structure or increasing its thermostability.

Authors: Bryan F Shaw; Haribabu Arthanari; Max Narovlyansky; Armando Durazo; Dominique P Frueh; Michael P Pollastri; Andrew Lee; Basar Bilgicer; Steven P Gygi; Gerhard Wagner; George M Whitesides
Journal: J Am Chem Soc Date: 2010-11-19 Impact factor: 15.419

10. Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.

Authors: J Clarke; A M Hounslow; M Bycroft; A R Fersht
Journal: Proc Natl Acad Sci U S A Date: 1993-11-01 Impact factor: 11.205

Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor.

1. Nativelike enzyme properties are important for optimum activity in neat organic solvents.

2. Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase.

3. NMR solution structure of the activation domain of human procarboxypeptidase A2.

4. Neutralizing positive charges at the surface of a protein lowers its rate of amide hydrogen exchange without altering its structure or increasing its thermostability.

5. The effect of low temperatures on enzyme activity.

Review 6. The denaturation and degradation of stable enzymes at high temperatures.

7. Genetic assignment of resonances in the NMR spectrum of a protein: lac repressor.

8. Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor.

9. Correlations between internal mobility and stability of globular proteins.

10. Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.