Interactions of phosphatidylinositol 3-kinase Src homology 3 domain with its ligand peptide studied by absorption, circular dichroism, and UV resonance raman spectroscopies.
about
Transient helical structure during PI3K and Fyn SH3 domain folding.Loop anchor modification causes the population of an alternative native state in an SH3-like domain.New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae
P2860
Interactions of phosphatidylinositol 3-kinase Src homology 3 domain with its ligand peptide studied by absorption, circular dichroism, and UV resonance raman spectroscopies.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Interactions of phosphatidylin ...... esonance raman spectroscopies.
@ast
Interactions of phosphatidylin ...... esonance raman spectroscopies.
@en
type
label
Interactions of phosphatidylin ...... esonance raman spectroscopies.
@ast
Interactions of phosphatidylin ...... esonance raman spectroscopies.
@en
prefLabel
Interactions of phosphatidylin ...... esonance raman spectroscopies.
@ast
Interactions of phosphatidylin ...... esonance raman spectroscopies.
@en
P2093
P2860
P1433
P1476
Interactions of phosphatidylin ...... esonance raman spectroscopies.
@en
P2093
P2860
P304
P356
10.1002/1097-0282(2000)57:4<208::AID-BIP2>3.0.CO;2-K
P577
2000-01-01T00:00:00Z