Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli.

Biomol NMR Assign. 2009 Dec;3(2):203-6. doi:10.1007/s12104-009-9175-3. Epub 2009 Jun 24

{{ author.authorName }}^{{{getOrganisationIndexOf(author)}}} {{ author.authorName }}^{{{getOrganisationIndexOf(author)}}}

+ et al

[No authors listed]

Author information

^{{index+1}} {{ organisation }}

摘要

We report the (1)H, (13)C and (15)N backbone chemical shift assignments and secondary structure of the Escherichia coli protein BamC, a 32-kDa protein subunit that forms part of the BAM (Omp85) complex, the beta-barrel assembly machinery present in all Gram-negative bacteria and which is essential for viability.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}

基因功能

{{$index+1}}.{{ gene }}

图表

‹ › ×

原始数据

保存测序数据

Sample name	Organism	Experiment title	Sample type	Library instrument	Attributes
Sample name	Organism	Experiment title	Sample type	Library instrument	{{attr}}
{{ dataList.sampleTitle }}	{{ dataList.organism }}	{{ dataList.expermentTitle }}	{{ dataList.sampleType }}	{{ dataList.libraryInstrument }}	{{ showAttributeName(index,attr,dataList.attributes) }}

Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli.

摘要

基因功能

图表

基因

原始数据

文献解读

分析平台

分析平台

分析流程

{{currentAnalyse.title}}