Structural studies of Mycobacterium tuberculosis Rv0899 reveal a monomeric membrane-anchoring protein with two separate domains
about
The non-catalytic "cap domain" of a mycobacterial metallophosphoesterase regulates its expression and localization in the cell.Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN(-) binding defined by EPR-based hybrid method.Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane ProteinsSolution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Distance measurement between two flexible sites in proteins in high viscosity medium at physiological temperature using continuous wave EPR.Efficient long-distance NMR-PRE and EPR-DEER restraints for two-domain protein structure determination.
P2860
Structural studies of Mycobacterium tuberculosis Rv0899 reveal a monomeric membrane-anchoring protein with two separate domains
description
2012 nî lūn-bûn
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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structural studies of Mycobact ...... tein with two separate domains
@ast
Structural studies of Mycobact ...... tein with two separate domains
@en
Structural studies of Mycobact ...... tein with two separate domains
@nl
type
label
Structural studies of Mycobact ...... tein with two separate domains
@ast
Structural studies of Mycobact ...... tein with two separate domains
@en
Structural studies of Mycobact ...... tein with two separate domains
@nl
prefLabel
Structural studies of Mycobact ...... tein with two separate domains
@ast
Structural studies of Mycobact ...... tein with two separate domains
@en
Structural studies of Mycobact ...... tein with two separate domains
@nl
P2093
P1476
Structural studies of Mycobact ...... tein with two separate domains
@en
P2093
Changlin Tian
Chaohua Lai
Chaowei Shi
Fangming Wu
P304
P356
10.1016/J.JMB.2011.11.016
P407
P577
2012-01-13T00:00:00Z