CD and 1H-NMR studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin.
about
An inducible helix-Gly-Gly-helix motif in the N-terminal domain of histone H1e: a CD and NMR studyHelicity of alpha(404-451) and beta(394-445) tubulin C-terminal recombinant peptidesSelf-association and domains of interactions of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by analytical ultracentrifugation and NMR experiments in trifluoroethanol/H(2)O mixtures.Position effect of cross-strand side-chain interactions on beta-hairpin formation.NMR and CD conformational studies of the C-terminal 16-peptides of Pseudomonas aeruginosa c551 and Hydrogenobacter thermophilus c552 cytochromes.Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site.NMR structural determinants of eosinophil cationic protein binding to membrane and heparin mimeticsConformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same foldConformationally driven protease-catalyzed splicing of peptide segments: V8 protease-mediated synthesis of fragments derived from thermolysin and ribonuclease A.The proprotein convertase SKI-1/S1P. In vitro analysis of Lassa virus glycoprotein-derived substrates and ex vivo validation of irreversible peptide inhibitors.A helix-turn motif in the C-terminal domain of histone H1.Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions.Empirical parameterization of a model for predicting peptide helix/coil equilibrium populations.Autonomous folding of a peptide corresponding to the N-terminal beta-hairpin from ubiquitinDNA-induced alpha-helical structure in the NH2-terminal domain of histone H1.Dynamics of the minimally frustrated helices determine the hierarchical folding of small helical proteins.Structural insight into the XTACC3/XMAP215 interaction from CD and NMR studies on model peptides.Solution conformation of an immunogenic peptide from HRV2: comparison with the conformation found in a complex with a Fab fragment of an anti-HRV2 neutralizing antibody.Structure-Activity Relationship of α Mating Pheromone from the Fungal Pathogen Fusarium oxysporum.CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.
P2860
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P2860
CD and 1H-NMR studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
CD and 1H-NMR studies on the c ...... erminal domain of thermolysin.
@ast
CD and 1H-NMR studies on the c ...... erminal domain of thermolysin.
@en
type
label
CD and 1H-NMR studies on the c ...... erminal domain of thermolysin.
@ast
CD and 1H-NMR studies on the c ...... erminal domain of thermolysin.
@en
prefLabel
CD and 1H-NMR studies on the c ...... erminal domain of thermolysin.
@ast
CD and 1H-NMR studies on the c ...... erminal domain of thermolysin.
@en
P2093
P2860
P50
P1433
P1476
CD and 1H-NMR studies on the c ...... terminal domain of thermolysin
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1993.TB17584.X
P407
P577
1993-02-01T00:00:00Z