The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase.
about
Optimization to low temperature activity in psychrophilic enzymesDefying the activity-stability trade-off in enzymes: taking advantage of entropy to enhance activity and thermostability.Role of disulfide bridges in the activity and stability of a cold-active alpha-amylaseNovel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome.Structure and function of cold shock proteins in archaea.Psychrophilic enzymes: from folding to function and biotechnology.Biotechnological uses of enzymes from psychrophiles.Characterisation of an L-haloacid dehalogenase from the marine psychrophile Psychromonas ingrahamii with potential industrial application.
P2860
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P2860
The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase.
description
2005 nî lūn-bûn
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2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2005年の論文
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name
The active site is the least s ...... in cold-adapted alpha-amylase.
@ast
The active site is the least s ...... in cold-adapted alpha-amylase.
@en
type
label
The active site is the least s ...... in cold-adapted alpha-amylase.
@ast
The active site is the least s ...... in cold-adapted alpha-amylase.
@en
prefLabel
The active site is the least s ...... in cold-adapted alpha-amylase.
@ast
The active site is the least s ...... in cold-adapted alpha-amylase.
@en
P2093
P2860
P1476
The active site is the least s ...... in cold-adapted alpha-amylase.
@en
P2093
Charles Gerday
Georges Feller
Khawar S Siddiqui
Laura Giaquinto
Salvino D'Amico
P2860
P304
P356
10.1128/JB.187.17.6197-6205.2005
P407
P577
2005-09-01T00:00:00Z