A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native beta-hairpin.
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Folding very short peptides using molecular dynamicsStructural characterization of a mutant peptide derived from ubiquitin: Implications for protein foldingTurn stability in β-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turnsβ-Strand Flipping and Slipping Triggered by Turn Replacement Reveal the Opportunistic Nature of β-Strand PairingEvolutionary Pareto-optimization of stably folding peptidesThe role of a beta-bulge in the folding of the beta-hairpin structure in ubiquitinAn improved capping unit for stabilizing the ends of associated β-strands.Molecular Simulations Find Stable Structures in Fragments of Protein G.Folding of small proteins using constrained molecular dynamicsMeasuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.Position effect of cross-strand side-chain interactions on beta-hairpin formation.Folding and stability of the three-stranded beta-sheet peptide Betanova: insights from molecular dynamics simulations.Cross-strand side-chain interactions versus turn conformation in beta-hairpinsCyclic modular beta-sheetsConformational studies of the C-terminal 16-amino-acid-residue fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. I. Importance of hydrophobic interactions in stabilization of beta-hairpin structure.Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin-binding protein G from Streptococcus. IV. Implication for the mechanism of folding of the parent protein.beta-hairpin-forming peptides; models of early stages of protein folding.A study of the influence of charged residues on β-hairpin formation by nuclear magnetic resonance and molecular dynamicsDesign of self-assembling peptide hydrogelators amenable to bacterial expressionProline-glutamate chimera's side chain conformation directs the type of β-hairpin structure.Like-charged residues at the ends of oligoalanine sequences might induce a chain reversal.Conformational 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 foldA molecular dynamics study of the 41-56 beta-hairpin from B1 domain of protein GThe turn sequence directs beta-strand alignment in designed beta-hairpins.Effects of turn residues in directing the formation of the beta-sheet and in the stability of the beta-sheet.A recipe for designing water-soluble, beta-sheet-forming peptides.Mutational effects on the folding dynamics of a minimized hairpin.Refolding simulations of an isolated fragment of barnase into a native-like beta hairpin: evidence for compactness and hydrogen bonding as concurrent stabilizing factors.Roles of beta-turns in protein folding: from peptide models to protein engineering.A designed beta-hairpin peptide in crystalsAnalysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet.A pH Switch for β-Sheet Protein Folding.Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor.Determinants of strand register in antiparallel beta-sheets of proteins.Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. III. Dynamics of long-range hydrophobic interactions.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.Assessing the Ability of Spectroscopic Methods to Determine the Difference in the Folding Propensities of Highly Similar β-Hairpins.Autonomous folding of a peptide corresponding to the N-terminal beta-hairpin from ubiquitin
P2860
Q21145688-EF79E2BD-B9CC-49E6-A5F0-F8502C8632C1Q27629222-8199F803-F980-4C65-BE0E-2EB1DBA566FDQ27640335-6393C5BD-910F-49CA-A338-8A0FF490E834Q27648967-3D514547-662E-438B-ABDA-438CA5DCB5A3Q27649880-D6E5B6FE-0634-4E25-8999-CF243045CBBBQ28359807-A4E4B0E1-C7D3-4062-ABDF-094C456BABA2Q30369170-E3D5ECD0-268A-4564-99AE-6FA0EC3C8B84Q30388894-E885D43C-D786-45F3-84EA-5489794C3768Q30402838-147C48D5-3E9C-42DD-B7C2-AF280325554CQ30500733-E5EE9D57-F782-4A15-8544-B18A2D288FC8Q30624796-85BED2A8-7842-49A6-9D52-EA2846505750Q30672007-A83A6AA2-9F06-4FC3-9FAE-48573E8408AEQ32161484-37AC7644-A1F1-42E4-B52A-036A2D26A7ECQ33273424-2C970546-4591-4D4B-BFDD-A9F0DF37E75DQ33365999-3F97C98A-5EE0-4FF5-9196-AFA7778A5CFDQ33393750-DFB8CD37-8554-483D-8A52-B4813748B774Q33691449-170815E3-0F83-43D5-A158-20655A06EEA3Q34005468-D0D0AEC5-9E7C-49D7-AB00-379ACBB610A1Q34553763-D225A1AF-53D8-4AE6-AE62-E5D4401D8722Q35032596-62E30319-722A-4672-B93C-131AB41EAC33Q35039690-591086FC-FECA-4703-B2E4-E8578FD7A52DQ36021320-1E43986D-AFE6-42DC-8C8D-DBDA64150B3EQ36280079-31EF4515-A128-4A5D-AE32-42273C71B5FEQ36281250-CA730C9C-FCBF-47C0-BD2C-91D9BCBFCD58Q36281322-0C0515D1-610D-433B-A5EA-0F898B1568B0Q36476507-C2EB8B63-A1C1-4672-BE79-F256C192B55CQ36821196-81A168E6-A452-4A70-A0FD-C5F9A469FFCCQ36823550-32214C23-645A-4A4F-80CB-42748E792003Q36885864-AF22D2BB-4896-4CCD-B6E9-FF094F5A056BQ37084770-5ADF20AA-B0CE-4598-8D53-24ECEAA808BCQ37395374-2A2FA464-06BF-4BD2-BE11-2DB09EAA0C54Q38269906-4DFA8B03-08BC-418C-9C85-AC3AC4752DF0Q41703997-7438D08E-C0A8-412B-91F4-5BB3EC2BC372Q41825662-D771AEE0-8C41-4C22-B817-8EF567293A83Q41915622-0641DE57-9F08-4458-BAB4-9EB7C5F29005Q42006079-6D15C91A-D5D3-4891-9466-3222C7C29754Q42121452-3A62568F-F5A9-47B9-AC3B-D60F640E0768Q42133852-9715337B-C829-4D77-A89F-EBB7233D6101Q42319098-0F063F50-3FCE-4CB4-ACD4-122FAB14404EQ42847121-24B9FD6A-A5B2-4FA6-B39C-540723CB9556
P2860
A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native beta-hairpin.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
A short linear peptide derived ...... table non-native beta-hairpin.
@ast
A short linear peptide derived ...... table non-native beta-hairpin.
@en
type
label
A short linear peptide derived ...... table non-native beta-hairpin.
@ast
A short linear peptide derived ...... table non-native beta-hairpin.
@en
prefLabel
A short linear peptide derived ...... table non-native beta-hairpin.
@ast
A short linear peptide derived ...... table non-native beta-hairpin.
@en
P2093
P2860
P356
P1476
A short linear peptide derived ...... table non-native beta-hairpin.
@en
P2093
Packman LC
Williams DH
P2860
P304
P356
10.1038/NSB1195-999
P577
1995-11-01T00:00:00Z