Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding.
about
Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solutionStructural characterization of a mutant peptide derived from ubiquitin: Implications for protein foldingNMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1The (1)H-NMR solution structure of the antitryptic core peptide of Bowman-Birk inhibitor proteins: a minimal canonical loopThe role of a beta-bulge in the folding of the beta-hairpin structure in ubiquitinFolding of a highly conserved diverging turn motif from the SH3 domain.The geometry and efficacy of cation-pi interactions in a diagonal position of a designed beta-hairpin.Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.Cross-strand interactions of fluorinated amino acids in β-hairpin constructs.Position effect of cross-strand side-chain interactions on beta-hairpin formation.Factors involved in the stability of isolated beta-sheets: Turn sequence, beta-sheet twisting, and hydrophobic surface burial.NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptideNanosecond temperature jump relaxation dynamics of cyclic beta-hairpin peptides.Sequence dependence of beta-hairpin structure: comparison of a salt bridge and an aromatic interaction.Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides.Crowding alone cannot account for cosolute effect on amyloid aggregationComparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation.Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study.The role of the unfolded state in hairpin stability.Cross-strand histidine-aromatic interactions enhance acyl-transfer rates in beta-hairpin peptide catalysts.Effects of turn residues in directing the formation of the beta-sheet and in the stability of the beta-sheet.α-helix to β-hairpin transition of human amylin monomer.Mutational effects on the folding dynamics of a minimized hairpin.Design of highly stabilized beta-hairpin peptides through cation-pi interactions of lysine and n-methyllysine with an aromatic pocketMinimization and optimization of designed beta-hairpin foldsSequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor.Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. II. Interplay of local backbone conformational dynamics and long-range hydrophobic interactions in hairpin formation.On the nucleation of amyloid beta-protein monomer folding.Terminal sidechain packing of a designed beta-hairpin influences conformation and stability.Investigation of the nature of the methionine-pi interaction in beta-hairpin peptide model systems.Diacid linkers that promote parallel beta-sheet secondary structure in water.Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns.Expected and unexpected results from combined beta-hairpin design elements.The role of plastic beta-hairpin and weak hydrophobic core in the stability and unfolding of a full sequence design protein.Exploring the conformational and biological versatility of β-turn-modified gramicidin S by using sugar amino acid homologues that vary in ring size.13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues.Conformational stabilization of a β-hairpin through a triazole-tryptophan interaction.Engineering β-sheets employing N-methylated heterochiral amino acids.On the intrinsic propensity of the Asn-Gly sequence to fold into type I' β-turn: molecular dynamics simulations of Asn-Gly β-turn containing peptide sequences.
P2860
Q21560956-6220A650-3F19-4276-9325-7EFA1619A7EAQ27629222-2AC0C364-621E-4068-83E8-6E5FAECB8D37Q27637271-3FA3769B-119E-4600-802F-E490BBC3DA26Q27639423-062F5006-FF1C-4762-9AAE-7EE6CBFE8498Q28359807-F89E34D2-9810-46F0-9FB7-AA7E91D83476Q30164860-65034026-AE9A-494A-BA35-C8B605ECA0A0Q30336215-FCC13F75-5012-43BD-AA31-ED001DEFECEAQ30443981-30324EC0-3276-4689-A461-56DBB46B52EBQ30573961-C3B99152-9882-4C67-9EA6-4B5AADF73970Q30624796-D016E40B-3D25-4FBC-A0C8-5B413812B909Q30916326-2679FFEB-3F58-47A2-97CA-A08DCBC024EBQ30989881-9BEEE1BB-B688-4CCC-AA6F-58F6D22B2C4DQ31027853-6DF285CB-3AEA-4CC7-A499-19F481537634Q33187175-3556F08E-8612-4234-935D-5A78DE3D57DCQ33195172-37C76416-CB1D-4473-AFD7-3C8027525D52Q33301065-55E84272-62B3-423C-97FD-25761A4CC676Q33798022-85E672BB-0AC1-4C48-9805-F77E9524B63BQ34030914-4790418B-273D-460A-AACB-8E64D2944EA1Q34155536-2F870DAC-FDB9-44A8-948F-3239561562B1Q34183835-4339F813-4808-469B-BA6A-E59A7CD3DDCEQ35276354-2C221246-3F70-4790-86FE-DF6E20353365Q36476507-FB2612EB-B90C-4064-A157-A71976255468Q36815150-2A834115-BE6E-4D8F-9218-CC05F357B373Q36823550-5F77BCF6-00C4-44D8-AA79-83A3E7860EFCQ37113747-BDD5507C-F20A-49C0-92A8-CCCFA6B90275Q38280257-CBFAA682-B492-4FB6-A29A-9E3F01D50D3EQ41915622-2E3F6E88-74B2-4BE7-B0B1-D85A31BD857FQ42133852-B28B4A0F-5FBE-49B8-BD6C-2F62787386F2Q42215600-A84C597A-DF9F-46EB-BBD7-C441CA1E5D74Q42872074-FB86F8FB-85CB-4963-98AA-E2D8D7174927Q43095134-A92C5DF0-2DD5-4DDB-B1FC-89DDC8F4EC17Q43119722-DB68EDCB-466B-4789-B010-00EB2F39B658Q44781090-80BF1A1F-62A6-4A67-A5EF-207B822A636CQ44978959-0920DB85-00B3-471E-AC55-E9FFE89046EAQ46168654-E4B845EC-C50E-4763-B138-9D765AAAAF62Q47388533-EC45800C-C8DD-4819-8598-F0D53A22B0BCQ48010445-D609BFC3-031E-4DF0-9C3C-FBE4C9CDE286Q48543667-90AE69C8-550A-49F4-90F3-83CADCDBAA21Q49955841-D52B73E3-5BEB-48F6-B0A3-A013BC20CC9CQ50020035-9F30BB4E-6368-4A1A-8C47-689C928338DC
P2860
Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Dissecting the stability of a ...... rand contributions to folding.
@ast
Dissecting the stability of a ...... rand contributions to folding.
@en
type
label
Dissecting the stability of a ...... rand contributions to folding.
@ast
Dissecting the stability of a ...... rand contributions to folding.
@en
altLabel
Dissecting the stability of a ...... ding 1 1Edited by P. E. Wright
@en
prefLabel
Dissecting the stability of a ...... rand contributions to folding.
@ast
Dissecting the stability of a ...... rand contributions to folding.
@en
P356
P1476
Dissecting the stability of a ...... rand contributions to folding.
@en
P2093
P304
P356
10.1006/JMBI.1999.3119
P407
P577
1999-10-01T00:00:00Z