Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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Pulling MscL open via N-terminal and TM1 helices: A computational study towards engineering an MscL nanovalve.Structural Dynamics of the MscL C-terminal Domain.Channel disassembled: Pick, tweak, and soak parts to soften.

P2860

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P2860

Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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Nanomechanical properties of MscL α helices: A steered molecular dynamics study.

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Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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Nanomechanical properties of MscL α helices: A steered molecular dynamics study.

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Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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Nanomechanical properties of MscL α helices: A steered molecular dynamics study.

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P1476

Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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P2093

A P Hill

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M Vossoughi

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N Bavi

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O Bavi

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R Naghdabadi

http://www.w3.org/2001/XMLSchema#string

Y Jamali

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P2860

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Structure and stability of the C-terminal helical bundle of theE. colimechanosensitive channel of large conductance

Membrane proteins bind lipids selectively to modulate their structure and function.

VMD: visual molecular dynamics

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209-223

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scholarly article

P356

10.1080/19336950.2016.1249077

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http://www.w3.org/2001/XMLSchema#string

P478

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Boris Martinac

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2016-10-18T00:00:00Z

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27753526

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Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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P2860

P2860

Nanomechanical properties of MscL α helices: A steered molecular dynamics study

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932