Cation-π interactions induce kinking of a molecular hinge in the RNA polymerase bridge-helix domain.
about
The Bridge Helix of RNA polymerase acts as a central nanomechanical switchboard for coordinating catalysis and substrate movementCations form sequence selective motifs within DNA grooves via a combination of cation-pi and ion-dipole/hydrogen bond interactions.The RNA polymerase bridge helix YFI motif in catalysis, fidelity and translocation.Antifragility and Tinkering in Biology (and in Business) Flexibility Provides an Efficient Epigenetic Way to Manage Risk.Hinge action versus grip in translocation by RNA polymerase.
P2860
Cation-π interactions induce kinking of a molecular hinge in the RNA polymerase bridge-helix domain.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on January 2011
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Cation-π interactions induce k ...... olymerase bridge-helix domain.
@en
Cation-π interactions induce k ...... olymerase bridge-helix domain.
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type
label
Cation-π interactions induce k ...... olymerase bridge-helix domain.
@en
Cation-π interactions induce k ...... olymerase bridge-helix domain.
@nl
prefLabel
Cation-π interactions induce k ...... olymerase bridge-helix domain.
@en
Cation-π interactions induce k ...... olymerase bridge-helix domain.
@nl
P2093
P2860
P356
P1476
Cation-π interactions induce k ...... olymerase bridge-helix domain.
@en
P2093
Gabor Terstyanszky
Hans Heindl
Noam Weingarten
Pamela Greenwell
Robert O J Weinzierl
Tamas Kiss
P2860
P356
10.1042/BST0390031
P577
2011-01-01T00:00:00Z