Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer
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Analysis of SecA dimerization in solution.Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Probing the Ion Binding Site in a DNA Holliday Junction Using Förster Resonance Energy Transfer (FRET).Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.An alternate mode of oligomerization for E. coli SecA.The Sec System: Protein Export in Escherichia coli.Driving Forces of Translocation Through Bacterial Translocon SecYEG.Alignment of the protein substrate hairpin along the SecA two-helix finger primes protein transport in Escherichia coli.SecA functions in vivo as a discrete anti-parallel dimer to promote protein transport.The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.
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P2860
Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer
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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 29 March 2013
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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
Defining the solution state di ...... ster resonance energy transfer
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Defining the solution state di ...... ter resonance energy transfer.
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Defining the solution state di ...... ster resonance energy transfer
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Defining the solution state di ...... ter resonance energy transfer.
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Defining the solution state di ...... ster resonance energy transfer
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Defining the solution state di ...... ter resonance energy transfer.
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P2093
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Defining the solution state di ...... ster resonance energy transfer
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Donald B Oliver
Ishita Mukerji
Sarah M Auclair
P2860
P304
P356
10.1021/BI301217T
P407
P577
2013-03-29T00:00:00Z