about
Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic coreSolution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopyHelix cappingAtypical DNA recognition mechanism used by the EspR virulence regulator of Mycobacterium tuberculosisA quantitative methodology for the de novo design of proteins.Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.Combinatorial redesign of the DNA binding specificity of a prokaryotic helix-turn-helix repressor.Classification of multi-helical DNA-binding domains and application to predict the DBD structures of sigma factor, LysR, OmpR/PhoB, CENP-B, Rapl, and Xy1S/Ada/AraC.Retroevolution of lambda Cro toward a stable monomer.Predicted common structural features of DNA-binding domains from Ets, Myb and HMG transcription factors.Functional domains of the AraC proteinDe novo design of the hydrophobic cores of proteins.Probing the protein-folding mechanism using denaturant and temperature effects on rate constantsStructural aspects of protein-DNA recognition.lac repressor: crystallization of intact tetramer and its complexes with inducer and operator DNAStructure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis.Common structural motifs in small proteins and domains.Mutant bZip-DNA complexes with four quasi-identical protein-DNA interfaces.Density-based score for selecting near-native atomic models of unknown structuresA comparative study of dynamic structures between phage 434 Cro and repressor proteins by normal mode analysis.Design and synthesis of sequence-specific DNA-binding peptides.Identifying native-like protein structures using physics-based potentials.
P2860
Q24564567-C7A8661D-BFC7-4BB0-A85E-E02432B9BC36Q24594007-EC563B4A-A550-4EA8-9ED5-BD11E23F57D1Q24673351-E1ED3ECD-2FFD-4BC9-AEC4-CCAF9D3CFCABQ27672757-49A2B95C-9396-432C-A803-203EAA4DC123Q30419165-86558C8E-819A-42CF-8688-89BFA57C3658Q30580694-21665E33-AAA8-4A2A-9D4C-6E42D429E8A4Q33185603-409AF7DB-A994-436A-8066-385FE78ECA93Q34057931-2BD8123B-89C1-4FAD-871C-A33924AA4AE5Q34805296-F71BB4F2-847E-4E45-9BD2-7AAAACD16633Q35016044-F62BF944-08F4-47C3-8F03-A5C39E9A0850Q36367901-F796BD51-C2A2-4B23-BABE-F5996CEA87F2Q36788061-E85E2C94-DDF8-4E27-AB6F-31976486499DQ37240517-C5B868D1-6891-40D5-9B6C-0B4709D12507Q37285869-DCC062DF-F3B0-4DF3-969D-5DC2A0B41E4EQ37711815-94692F79-4793-4F87-8E22-3674BBEEF090Q40018615-F75B4498-C32D-45C1-9DC0-A20B986D4C0DQ40648819-816313DB-54D9-46D4-A856-8F01A808FDFAQ41063863-751B977D-6B5F-4668-A83A-778AA8FD1B31Q42063957-B880D250-F664-47B4-9F45-EE43979A8E3DQ44686524-B64AA900-846B-439B-A19F-B6509DE080F2Q45042387-4465F425-C4C5-4ACD-B02F-945CA5FFF272Q46165830-6625A386-B41D-46E6-9BFA-608AF717CDE4
P2860
description
1989 nî lūn-bûn
@nan
1989 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Structure of phage 434 Cro protein at 2.35 A resolution
@ast
Structure of phage 434 Cro protein at 2.35 A resolution
@en
Structure of phage 434 Cro protein at 2.35 A resolution
@nl
type
label
Structure of phage 434 Cro protein at 2.35 A resolution
@ast
Structure of phage 434 Cro protein at 2.35 A resolution
@en
Structure of phage 434 Cro protein at 2.35 A resolution
@nl
prefLabel
Structure of phage 434 Cro protein at 2.35 A resolution
@ast
Structure of phage 434 Cro protein at 2.35 A resolution
@en
Structure of phage 434 Cro protein at 2.35 A resolution
@nl
P2093
P1476
Structure of phage 434 Cro protein at 2.35 A resolution
@en
P2093
A Mondragón
C Wolberger
S C Harrison
P304
P356
10.1016/0022-2836(89)90374-4
P407
P577
1989-01-05T00:00:00Z