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10 in total

1. C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.

Authors: Matthew J Gage; Anne Skaja Robinson
Journal: Protein Sci Date: 2003-12 Impact factor: 6.725

2. Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.

Authors: Brian G Lefebvre; Noelle K Comolli; Matthew J Gage; Anne Skaja Robinson
Journal: Protein Sci Date: 2004-05-07 Impact factor: 6.725

3. Three amino acids that are critical to formation and stability of the P22 tailspike trimer.

Authors: Matthew J Gage; Jennifer L Zak; Anne Skaja Robinson
Journal: Protein Sci Date: 2005-08-04 Impact factor: 6.725

4. Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.

Authors: S D Betts; J King
Journal: Protein Sci Date: 1998-07 Impact factor: 6.725

5. Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies.

Authors: M A Speed; T Morshead; D I Wang; J King
Journal: Protein Sci Date: 1997-01 Impact factor: 6.725

6. Identification of sites influencing the folding and subunit assembly of the P22 tailspike polypeptide chain using nonsense mutations.

Authors: B Fane; J King
Journal: Genetics Date: 1987-10 Impact factor: 4.562

Review 7. Protein engineering. The design, synthesis and characterization of factitious proteins.

Authors: W V Shaw
Journal: Biochem J Date: 1987-08-15 Impact factor: 3.857

8. Nonnative interactions between cysteines direct productive assembly of P22 tailspike protein.

Authors: Brenda L Danek; Anne Skaja Robinson
Journal: Biophys J Date: 2003-11 Impact factor: 4.033

9. Kinetic folding studies of the P22 tailspike beta-helix domain reveal multiple unfolded states.

Authors: M L Spatara; C J Roberts; A S Robinson
Journal: Biophys Chem Date: 2009-02-12 Impact factor: 3.628

10. Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state.

Authors: Tatiana N Melnik; Maria A Majorina; Daria S Larina; Ivan A Kashparov; Ekaterina N Samatova; Anatoly S Glukhov; Bogdan S Melnik
Journal: PLoS One Date: 2014-06-03 Impact factor: 3.240

10 in total