A method to rationally increase protein stability based on the charge-charge interaction, with application to lipase LipK107.
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Improvement in Thermostability of an Achaetomium sp. Strain Xz8 Endopolygalacturonase via the Optimization of Charge-Charge Interactions.Improvement of the thermostability and catalytic efficiency of a highly active β-glucanase from Talaromyces leycettanus JCM12802 by optimizing residual charge-charge interactions.Engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency.Salt bridge as a gatekeeper against partial unfolding.
P2860
A method to rationally increase protein stability based on the charge-charge interaction, with application to lipase LipK107.
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2013 nî lūn-bûn
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2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
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2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
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name
A method to rationally increas ...... application to lipase LipK107.
@ast
A method to rationally increas ...... application to lipase LipK107.
@en
type
label
A method to rationally increas ...... application to lipase LipK107.
@ast
A method to rationally increas ...... application to lipase LipK107.
@en
prefLabel
A method to rationally increas ...... application to lipase LipK107.
@ast
A method to rationally increas ...... application to lipase LipK107.
@en
P2093
P2860
P356
P1433
P1476
A method to rationally increas ...... application to lipase LipK107.
@en
P2093
Dongbing Cui
Dongzhi Wei
Lujia Zhang
Shuiqin Jiang
Xiaomang Tang
Y Adam Yuan
Zhiqiang Yao
P2860
P304
P356
10.1002/PRO.2388
P577
2013-11-22T00:00:00Z