Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9.
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The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.Basis of Protein Stabilization by K Glutamate: Unfavorable Interactions with Carbon, Oxygen Groups.Protein folding on biosensor tips: folding of maltodextrin glucosidase monitored by its interactions with GroEL.The mechanism and high-free-energy transition state of lac repressor-lac operator interaction.Glutamate promotes SSB protein-protein Interactions via intrinsically disordered regions.Protein Cofactors Are Essential for High-Affinity DNA Binding by the Nuclear Factor κB RelA Subunit.
P2860
Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9.
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2016 nî lūn-bûn
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2016年の論文
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2016年論文
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2016年論文
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2016年論文
@zh-hk
2016年論文
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2016年論文
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2016年论文
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2016年论文
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2016年论文
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name
Positioning the Intracellular ...... cal Unfolding Studies of NTL9.
@ast
Positioning the Intracellular ...... cal Unfolding Studies of NTL9.
@en
type
label
Positioning the Intracellular ...... cal Unfolding Studies of NTL9.
@ast
Positioning the Intracellular ...... cal Unfolding Studies of NTL9.
@en
prefLabel
Positioning the Intracellular ...... cal Unfolding Studies of NTL9.
@ast
Positioning the Intracellular ...... cal Unfolding Studies of NTL9.
@en
P2093
P2860
P1433
P1476
Positioning the Intracellular ...... cal Unfolding Studies of NTL9.
@en
P2093
Adrian Pantel
Irina Shkel
Ivan Peran
M Thomas Record
Natalie Stenzoski
Rituparna Sengupta
Xian Cheng
P2860
P304
P356
10.1021/ACS.BIOCHEM.6B00173
P407
P577
2016-04-07T00:00:00Z