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Literature DB >> 1412703

Protein engineering.

Abstract

Ten years of protein engineering have seen the synthesis of novel therapeutic agents and the analysis of the structure, activity, specificity, stability and folding pathways of proteins. It is hoped that protein engineering will eventually lead to the design of novel catalytic sites on either novel or existing proteins.

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Year: 1992 PMID： 1412703 DOI： 10.1016/0968-0004(92)90438-f

Source DB: PubMed Journal: Trends Biochem Sci ISSN： 0968-0004 Impact factor: 13.807

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Cited

14 in total

1. Pressure effects on the proximal heme pocket in myoglobin probed by Raman and near-infrared absorption spectroscopy.

Authors: O Galkin; S Buchter; A Tabirian; A Schulte
Journal: Biophys J Date: 1997-11 Impact factor: 4.033

2. Homogenates of yeast cultures with engineered catalases F148V and V111A reveal higher specific activities after incubation at permissive temperature.

Authors: M Zámocký; F Koller
Journal: Folia Microbiol (Praha) Date: 1997 Impact factor: 2.099

3. Engineering subunit association of multisubunit proteins: a dimeric streptavidin.

Authors: T Sano; S Vajda; C L Smith; C R Cantor
Journal: Proc Natl Acad Sci U S A Date: 1997-06-10 Impact factor: 11.205

4. Flexibility of the "rigid" classics or rugged bottom of the folding funnels of myoglobin, lysozyme, RNase A, chymotrypsin, cytochrome c, and carboxypeptidase A1.

Authors: Vladimir N Uversky
Journal: Intrinsically Disord Proteins Date: 2017-10-16

10. Incorporation of the fluorescent amino acid 7-azatryptophan into the core domain 1-47 of hirudin as a probe of hirudin folding and thrombin recognition.

Authors: Vincenzo De Filippis; Silvia De Boni; Elisa De Dea; Daniele Dalzoppo; Claudio Grandi; Angelo Fontana
Journal: Protein Sci Date: 2004-06 Impact factor: 6.725

Protein engineering.

1. Pressure effects on the proximal heme pocket in myoglobin probed by Raman and near-infrared absorption spectroscopy.

2. Homogenates of yeast cultures with engineered catalases F148V and V111A reveal higher specific activities after incubation at permissive temperature.

3. Engineering subunit association of multisubunit proteins: a dimeric streptavidin.

4. Flexibility of the "rigid" classics or rugged bottom of the folding funnels of myoglobin, lysozyme, RNase A, chymotrypsin, cytochrome c, and carboxypeptidase A1.

Review 5. The molecular basis of genetic dominance.

6. A quantitative methodology for the de novo design of proteins.

7. Bacteriophage T4 as a surface display vector.

Review 8. Biological messiness vs. biological genius: Mechanistic aspects and roles of protein promiscuity.

9. Cold denaturation of a protein dimer monitored at atomic resolution.

10. Incorporation of the fluorescent amino acid 7-azatryptophan into the core domain 1-47 of hirudin as a probe of hirudin folding and thrombin recognition.