Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.
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Identification of lipopolysaccharide-binding peptide regions within HMGB1 and their effects on subclinical endotoxemia in a mouse modelLDL receptor/lipoprotein recognition: endosomal weakening of ApoB and ApoE binding to the convex face of the LR5 repeatThermodynamic analysis of Jun-Fos coiled coil peptide antagonistsProthymosin alpha interacts with the CREB-binding protein and potentiates transcription.A helix propensity scale based on experimental studies of peptides and proteinsIMP dehydrogenase: structure, mechanism, and inhibition.All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples.Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studiesStructural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein foldingThermodynamic and structural characterization of Asn and Ala residues in the disallowed II′ region of the Ramachandran plotIntegrated Modeling Program, Applied Chemical Theory (IMPACT)NMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain.Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure.Protein secondary structure and stability determined by combining exoproteolysis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.Rapid search for tertiary fragments reveals protein sequence-structure relationshipsStructural and Functional Insights into the Cryoprotection of Membranes by the Intrinsically Disordered DehydrinsTertiary alphabet for the observable protein structural universe.Direct ubiquitin independent recognition and degradation of a folded protein by the eukaryotic proteasomes-origin of intrinsic degradation signals.Toward an improved structural model of the frog-skin antimicrobial peptide esculentin-1b(1-18).Self-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.Thermodynamic analysis of helix-engineered forms of the activation domain of human procarboxypeptidase A2.Interaction of a designed interleukin-10 epitope mimic with an antibody studied by isothermal titration microcalorimetry.Sequence analysis of an artificial family of RNA-binding peptidesConformational studies of the alpha-helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.Electrostatic contacts in the activator protein-1 coiled coil enhance stability predominantly by decreasing the unfolding rate.Structural and antimicrobial properties of human pre-elafin/trappin-2 and derived peptides against Pseudomonas aeruginosa.Phi values in protein-folding kinetics have energetic and structural components.Truncation, randomization, and selection: generation of a reduced length c-Jun antagonist that retains high interaction stabilityMembrane-active peptides: binding, translocation, and flux in lipid vesicles.Hydrogen bonding stabilizes globular proteins.Prepaying the entropic cost for allosteric regulation in KIXPrimary peptide folding dynamics observed with ultrafast temperature jumpA thermodynamic approach to the mechanism of cell-penetrating peptides in model membranesStructural divergence is more extensive than sequence divergence for a family of intrinsically disordered proteins.Structural basis of α-catenin recognition by EspB from enterohaemorrhagic E. coli based on hybrid strategy using low-resolution structural and protein dissection.Peptides in apoptosis research.Estimated secondary structure propensities within V1/V2 region of HIV gp120 are an important global antibody neutralization sensitivity determinant.What determines the activity of antimicrobial and cytolytic peptides in model membranesRational redesign of the folding pathway of a modular protein
P2860
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P2860
Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh-hant
name
Elucidating the folding proble ...... l content of natural peptides.
@en
Elucidating the folding proble ...... l content of natural peptides.
@nl
type
label
Elucidating the folding proble ...... l content of natural peptides.
@en
Elucidating the folding proble ...... l content of natural peptides.
@nl
prefLabel
Elucidating the folding proble ...... l content of natural peptides.
@en
Elucidating the folding proble ...... l content of natural peptides.
@nl
P356
P1476
Elucidating the folding proble ...... l content of natural peptides.
@en
P2093
P304
P356
10.1006/JMBI.1994.0023
P407
P577
1995-01-01T00:00:00Z