Incorporating beta-turns and a turn mimetic out of context in loop 1 of the WW domain affords cooperatively folded beta-sheets.
about
Structure-function-folding relationship in a WW domainEvaluating beta-turn mimics as beta-sheet folding nucleatorsProtein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structureUsing flexible loop mimetics to extend -value analysis to secondary structure interactionsNMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1Conformationally stable and constrained macrocarbocyclic pseudopeptide mimics of beta-hairpin structures.Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation.Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and foldingRedesign of a WW domain peptide for selective recognition of single-stranded DNA.Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contextsContext-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.Temperature-dependent folding pathways of Pin1 WW domain: an all-atom molecular dynamics simulation of a Gō model.N-glycosylation of enhanced aromatic sequons to increase glycoprotein stabilityTowards "bionic" proteins: replacement of continuous sequences from HIF-1α with proteomimetics to create functional p300 binding HIF-1α mimics.Constrained peptides as miniature protein structuresDesign and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains.Reinvestigation of the proposed folding and self-association of the Neuropeptide Head Activator.Sequence determinants of thermodynamic stability in a WW domain--an all-beta-sheet protein.A PEG-based oligomer as a backbone replacement for surface-exposed loops in a protein tertiary structure.Expected and unexpected results from combined beta-hairpin design elements.Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Foldamer Tertiary Structure through Sequence-Guided Protein Backbone Alteration.Probing the ligand-binding specificity and analyzing the folding state of SPOT-synthesized FBP28 WW domain variants.Protein stabilization by tuning the steric restraint at the reverse turn† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7sc05163h.
P2860
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P2860
Incorporating beta-turns and a turn mimetic out of context in loop 1 of the WW domain affords cooperatively folded beta-sheets.
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2001 nî lūn-bûn
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name
Incorporating beta-turns and a ...... peratively folded beta-sheets.
@en
Incorporating beta-turns and a ...... peratively folded beta-sheets.
@nl
type
label
Incorporating beta-turns and a ...... peratively folded beta-sheets.
@en
Incorporating beta-turns and a ...... peratively folded beta-sheets.
@nl
prefLabel
Incorporating beta-turns and a ...... peratively folded beta-sheets.
@en
Incorporating beta-turns and a ...... peratively folded beta-sheets.
@nl
P2093
P356
P1476
Incorporating beta-turns and a ...... peratively folded beta-sheets.
@en
P2093
P304
P356
10.1021/JA0102890
P407
P577
2001-06-01T00:00:00Z