A natural and readily available crowding agent: NMR studies of proteins in hen egg white
about
Specific ion effects on macromolecular interactions in Escherichia coli extracts.An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states.Difference between Extra- and Intracellular T1 Values of Carboxylic Acids Affects the Quantitative Analysis of Cellular Kinetics by Hyperpolarized NMR.Cell lysates and egg white create homeostatic microenvironment for gene expression in cell-free system
P2860
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@ast
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@en
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@nl
type
label
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@ast
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@en
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@nl
prefLabel
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@ast
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@en
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@nl
P2093
P2860
P356
P1433
P1476
A natural and readily available crowding agent: NMR studies of proteins in hen egg white
@en
P2093
Gabriel Martorell
Miquel Adrover
Piero Andrea Temussi
P2860
P304
P356
10.1002/PROT.22967
P407
P577
2011-05-01T00:00:00Z