The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics.
about
Solution NMR Structures of Productive and Non-productive Complexes between the A and B Domains of the Cytoplasmic Subunit of the Mannose Transporter of the Escherichia coli Phosphotransferase SystemThe polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamicsStructural basis of RGD-hirudin binding to thrombin: Tyr3 and five C-terminal residues are crucial for inhibiting thrombin activity.Protein engineering. The design, synthesis and characterization of factitious proteins.Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibitionChanges in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms.
P2860
The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics.
description
1987 nî lūn-bûn
@nan
1987 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
The conformations of hirudin i ...... restrained molecular dynamics.
@ast
The conformations of hirudin i ...... restrained molecular dynamics.
@en
type
label
The conformations of hirudin i ...... restrained molecular dynamics.
@ast
The conformations of hirudin i ...... restrained molecular dynamics.
@en
prefLabel
The conformations of hirudin i ...... restrained molecular dynamics.
@ast
The conformations of hirudin i ...... restrained molecular dynamics.
@en
P2093
P2860
P1433
P1476
The conformations of hirudin i ...... restrained molecular dynamics
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1987.TB04785.X
P407
P577
1987-02-01T00:00:00Z