The quest for molecular quasi-species in ligand-activity space and its application to directed enzyme evolution.
about
Probing the activity modification space of the cysteine peptidase cathepsin K with novel allosteric modifiersTailor-made biocatalysts: combining thermodynamics, organic synthesis, molecular biology, biochemistry and microbiology for the design of enzyme selections.Enhancing the thermal robustness of an enzyme by directed evolution: least favorable starting points and inferior mutants can map superior evolutionary pathways.Specificity Effects of Amino Acid Substitutions in Promiscuous Hydrolases: Context-Dependence of Catalytic Residue Contributions to Local Fitness Landscapes in Nearby Sequence Space.Clusters of Multiple Mutations: Incidence and Molecular MechanismsCatalytic versus inhibitory promiscuity in cytochrome P450s: implications for evolution of new function.
P2860
The quest for molecular quasi-species in ligand-activity space and its application to directed enzyme evolution.
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The quest for molecular quasi- ...... to directed enzyme evolution.
@ast
The quest for molecular quasi- ...... to directed enzyme evolution.
@en
type
label
The quest for molecular quasi- ...... to directed enzyme evolution.
@ast
The quest for molecular quasi- ...... to directed enzyme evolution.
@en
prefLabel
The quest for molecular quasi- ...... to directed enzyme evolution.
@ast
The quest for molecular quasi- ...... to directed enzyme evolution.
@en
P2860
P1433
P1476
The quest for molecular quasi- ...... to directed enzyme evolution.
@en
P2093
Arna Runarsdottir
Bengt Mannervik
P2860
P304
P356
10.1016/J.FEBSLET.2010.04.024
P407
P577
2010-04-18T00:00:00Z