Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins.
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Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a proteinBayesian model aggregation for ensemble-based estimates of protein pKa values.The single T65S mutation generates brighter cyan fluorescent proteins with increased photostability and pH insensitivity.The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model.
P2860
Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins.
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年學術文章
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2011年學術文章
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2011年學術文章
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name
Thermodynamic principles for t ...... and acid insensitive proteins.
@en
Thermodynamic principles for t ...... and acid insensitive proteins.
@nl
type
label
Thermodynamic principles for t ...... and acid insensitive proteins.
@en
Thermodynamic principles for t ...... and acid insensitive proteins.
@nl
prefLabel
Thermodynamic principles for t ...... and acid insensitive proteins.
@en
Thermodynamic principles for t ...... and acid insensitive proteins.
@nl
P2093
P2860
P1476
Thermodynamic principles for t ...... and acid insensitive proteins
@en
P2093
Aaron C Robinson
Bertrand García-Moreno E
Erika L Wheeler
Janine Lin
Peregrine Bell-Upp
Steven T Whitten
P2860
P304
P356
10.1016/J.BPC.2011.06.016
P577
2011-07-07T00:00:00Z