Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding

Protein Science

Volumn 9, Issue 11, 2000, Pages 2142-2150

  Zerella, Rosa ^a   Williams, Dudley H ^a   Chen, Pei Yeh ^a,b   Evans, Philip A ^a   Raine, Andrew ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b INSTITUTE OF CHEMISTRY   (Taiwan)

Author keywords

NMR; Peptide; Peptide conformations; Structure; Ubiquitin; X PLOR; hairpin; sheet

Indexed keywords

AMINO ACID; ASPARTIC ACID; LYSINE; MUTANT PROTEIN; THREONINE; UBIQUITIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; GENE MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

EID: 0034489543     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.11.2142     Document Type: Article

References (30)

1. A short linear peptide that folds into a native stable β-hairpin in aqueous-solution
2. Coherence transfer by isotropic mixing - Application to proton correlation spectroscopy
3. Dissecting the structure of a partially folded protein - Circular-dichroism and NMR studies of peptides from ubiquitin
4. The turn sequence directs β-strand alignment in designed β-hairpins
5. Dissecting the stability of a β-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the β-turn and β-strand contributions to folding
6. Modulation of intrinsic phi, psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a β-hairpin peptide
7. Characterization of a partially denatured state of a protein by 2-dimensional NMR - Reduction of the hydrophobic interactions in ubiquitin
8. Determinants of strand register in antiparallel β-sheets of proteins
9. A revised set of potentials for β-turn formation in proteins
10. Investigation of exchange processes by two-dimensional NMR spectroscopy
11. Evidence for a 3-state model of protein folding from kinetic-analysis of ubiquitin variants with altered core residues
12. PROCHECK: A program to check the stereochemical quality of protein structures
13. Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
14. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of H1-H1 spin-spin coupling-constants in proteins
15. Folding dynamics and mechanism of β-hairpin formation
16. Multiple quantum filters for elucidating NMR coupling networks
17. Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous-solutions
18. How does protein synthesis give rise to the 3D-structure
19. Role of β-turn residues in β-hairpin formation and stability in designed peptides
20. De-novo design and structural-analysis of a model β-hairpin peptide system
21. β-hairpin and β-sheet formation in designed linear peptides
22. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin
23. Guidelines for protein design - The energetics of β-sheet side chain interactions
24. Heteronuclear 3-dimensional NMR-spectroscopy of a partially denatured protein - The A-state of human ubiquitin
25. Measurement of homonuclear coupling-constants from NMR correlation spectra
26. An analysis of side chain interactions and pair correlations within antiparallel β-sheets - The difference between backbone hydrogen-bonded nad non-hydrogen-bonded residue pairs
27. Autonomous folding of a peptide corresponding to the N-terminal β-hairpin from ubiquitin