Engineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.

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Combinatorial Labeling Method for Improving Peptide Fragmentation in Mass Spectrometry.Protein deamidation in biopharmaceutical manufacture: understanding, control and impact

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Engineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.

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2014 nî lūn-bûn

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Engineering deamidation-suscep ...... o thermal cycling in a lipase.

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Engineering deamidation-suscep ...... o thermal cycling in a lipase.

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Engineering deamidation-suscep ...... o thermal cycling in a lipase.

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Engineering deamidation-suscep ...... o thermal cycling in a lipase.

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Engineering deamidation-suscep ...... o thermal cycling in a lipase.

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Engineering deamidation-suscep ...... o thermal cycling in a lipase.

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P1476

Engineering deamidation-suscep ...... o thermal cycling in a lipase.

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P2093

K Bhanuramanand

http://www.w3.org/2001/XMLSchema#string

N M Rao

http://www.w3.org/2001/XMLSchema#string

Shoeb Ahmad

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P2860

Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin

Thermostable Bacillus subtilis lipases: in vitro evolution and structural insight

In vitro evolved non-aggregating and thermostable lipase: structural and thermodynamic investigation

Deamidation in proteins: the crystal structure of bovine pancreatic ribonuclease with an isoaspartyl residue at position 67

The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage

Simultaneous assessment of Asp isomerization and Asn deamidation in recombinant antibodies by LC-MS following incubation at elevated temperatures

Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals?

Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaB-crystallin.

Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.

Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis.

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1479-1490

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scholarly article

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10.1002/PRO.2516

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2014-08-05T00:00:00Z

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Engineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.

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P2860

P2860

Engineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.

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