about
Protein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structureMagnetotactic molecular architectures from self-assembly of β-peptide foldamers.A modular toolkit to inhibit proline-rich motif-mediated protein-protein interactions.Peptide-functionalized semiconductor surfaces: strong surface electronic effects from minor alterations to backbone composition.Robust helix formation in a new family of oligoureas based on a constrained bicyclic building block.Hairpin formation promoted by the heterochiral dinipecotic acid segment: A DFT study.Evaluation of a cyclopentane-based γ-amino acid for the ability to promote α/γ-peptide secondary structure.Orthanilic acid-promoted reverse turn formation in peptides.Peptidomimetics via modifications of amino acids and peptide bonds.GLUE that sticks to HIV: a helix-grafted GLUE protein that selectively binds the HIV gp41 N-terminal helical region.Intrinsic Folding Proclivities in Cyclic β-Peptide Building Blocks: Configuration and Heteroatom Effects Analyzed by Conformer-Selective Spectroscopy and Quantum Chemistry.Conformational properties of 1,4- and 1,5-substituted 1,2,3-triazole amino acids – building units for peptidic foldamersComparison of design strategies for α-helix backbone modification in a protein tertiary fold.Efficient continuous-flow synthesis of novel 1,2,3-triazole-substituted β-aminocyclohexanecarboxylic acid derivatives with gram-scale productionMolecules that mimic apolipoprotein A-I: potential agents for treating atherosclerosis.A compendium of cyclic sugar amino acids and their carbocyclic and heterocyclic nitrogen analogues.Development of protein mimics for intracellular delivery.Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.An overview of peptide and peptoid foldamers in medicinal chemistry.Homochirality of β-Peptides: A Significant Biomimetic Property of Unnatural Systems.Integrin Ligands with α/β-Hybrid Peptide Structure: Design, Bioactivity, and Conformational Aspects.Right-Handed Helical Foldamers Consisting of De Novo d-AApeptides.The importance of being Aib. Aggregation and self-assembly studies on conformationally constrained oligopeptides.Sulfono-γ-AApeptides as a new class of nonnatural helical foldamer.Polymeric Tubular Aromatic Amide Helices.Chiral Nanotubes.Self-assembled vesicles of urea-tethered foldamers as hydrophobic drug carriers.Origin of problems related to Staudinger reduction in carbopeptoid syntheses.Protein prosthesis: β-peptides as reverse-turn surrogates.Dynamic combinatorial enrichment of polyconformational D-/L-peptide dimers.Native like helices in a specially designed β peptide in the gas phase.Conformational modulation of peptides using β-amino benzenesulfonic acid ((S)Ant).β- and γ-Amino Acids at α-Helical Interfaces: Toward the Formation of Highly Stable Foldameric Coiled Coils.Slow folding-unfolding kinetics of an octameric β-peptide bundle.Synthesis of hybrid hydrazino peptides: protected vs unprotected chiral α-hydrazino acids.A practical route to β(2,3)-amino acids with alkyl side chainsEfficient regio- and stereoselective access to novel fluorinated β-aminocyclohexanecarboxylates.Stereoselective synthesis of perillaldehyde-based chiral β-amino acid derivatives through conjugate addition of lithium amides.Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid.Switching the H-bonding network of a foldamer by modulating the backbone chirality and constitutional ratio of amino acids.
P2860
Q26852997-61B21219-E719-42B2-8309-6AB0C0539676Q27319476-C3923A6E-DF63-4D66-B856-FB85A957E1E6Q30009193-BDEDB67F-2FC2-4F47-B3F0-6115F6A1A6D5Q30398525-6E995D10-6CBE-43B3-BB3B-8F3751D8E8C2Q30572112-957CC3BF-22CE-430F-99C6-6C8149E2B174Q30959508-048D4E9F-9253-46AB-A0BC-7261C3206963Q33942772-C108831F-225B-4723-992A-EFD97902C28FQ34326814-31579668-918A-4A1D-B505-E1E06EAE61D3Q35120205-83147849-3580-4DE7-9620-384DEAC7D4CDQ35751518-81EE969A-4445-459E-B49E-0DB04401A7AFQ35788290-AD9C5542-39E5-4377-AFE4-ABA559490C94Q36477775-CA9FF275-2A50-488D-B53B-CB10DC84DF1CQ36619907-725D0FC0-1B6F-45D7-AD3B-93AB8C59751EQ37088102-0B3130EA-4C1A-4D1A-9448-C393DCB0FF28Q37671683-7F7CE5BC-1EEA-4B6E-8CED-68F350FE3391Q38129764-AD448D7A-46E4-4C01-8664-011F510BAED3Q38413685-C22DEBB6-F3ED-4199-A3A0-7F63A9D9432BQ38539666-88ED9EBD-B20A-40F8-B4E2-62EDE5349AF0Q38569751-5E2AEF8F-C464-4311-B12F-CB22E19F2358Q38644625-71081EC9-C073-4A92-B277-E9A9241EE1DDQ38700087-38D762AF-76A2-48F5-9F57-86F1F1391DC7Q38798838-D0272527-05CB-4562-8F97-DC41F7AABA95Q39068065-45F67867-9C45-4BFB-81CA-8F0C150CEAB1Q39076733-C45BCBDA-C92A-4D45-B110-E4795BE486BDQ39344094-462000C1-C1D0-4384-B429-3E4DDA8AB221Q39414853-473F3F3A-3E51-439B-A10A-E9D5C66BCAECQ39502211-6654C75D-B85F-4449-9005-21347B3D8D2BQ39580760-CE9ADC30-22B6-401E-BCB1-D851F382A7D4Q41220419-FC0487AA-A648-4725-9709-2EF475F6B18FQ41357416-CC02ECC6-32EC-46AE-BDCB-FB303236CB17Q41543951-F158B800-4C9C-4707-A284-C571F85A80A2Q41677625-F286DF34-AA10-423E-A25A-83E3A74259BFQ41680082-4F4F1BB7-CFC6-4606-B82B-1BC82EE96493Q41790015-023ED2C7-97F0-407F-AD25-A580EDF35DBDQ41876335-F47B26FA-0302-4BCB-9B1F-11A5DD724C35Q41991216-BF01F7BB-7DEB-49DD-89BE-05FFA2FA1B87Q42239696-FF7BD6F2-0D0E-41D7-9F4B-AF143D2390F4Q43075307-8209928D-03F7-41E5-9DA2-6EDFB0DBDBF5Q43449759-FD57D495-EFD3-48C3-938C-36CB61F0C3B0Q43595570-62CD4A31-F307-4237-89A2-AAFF2EA23CB3
P2860
description
2012 nî lūn-bûn
@nan
2012 թուականին հրատարակուած գիտական յօդուած
@hyw
2012 թվականին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Peptidic foldamers: ramping up diversity
@ast
Peptidic foldamers: ramping up diversity
@en
type
label
Peptidic foldamers: ramping up diversity
@ast
Peptidic foldamers: ramping up diversity
@en
prefLabel
Peptidic foldamers: ramping up diversity
@ast
Peptidic foldamers: ramping up diversity
@en
P2860
P356
P1476
Peptidic foldamers: ramping up diversity
@en
P2093
Tamás A. Martinek
P2860
P304
P356
10.1039/C1CS15097A
P50
P577
2012-01-01T00:00:00Z