Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation.
about
Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engineCharacterization of disulfide bonds by planned digestion and tandem mass spectrometry.Mass spectrometry profiles superoxide-induced intramolecular disulfide in the FMN-binding subunit of mitochondrial Complex IAquatic proteins with repetitive motifs provide insights to bioengineering of novel biomaterials.One short cysteine-rich sequence pattern - two different disulfide-bonded structures - a molecular dynamics simulation study.QuanPol: a full spectrum and seamless QM/MM program.
P2860
Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Determination of a high-precis ...... its disulfide bond formation.
@en
Determination of a high-precis ...... its disulfide bond formation.
@nl
type
label
Determination of a high-precis ...... its disulfide bond formation.
@en
Determination of a high-precis ...... its disulfide bond formation.
@nl
prefLabel
Determination of a high-precis ...... its disulfide bond formation.
@en
Determination of a high-precis ...... its disulfide bond formation.
@nl
P2860
P50
P1433
P1476
Determination of a high-precis ...... its disulfide bond formation.
@en
P2093
Elena Pokidysheva
Hans Peter Bächinger
P2860
P304
P356
10.1016/J.FEBSLET.2004.05.034
P407
P577
2004-07-01T00:00:00Z