Influence of strand number on antiparallel beta-sheet stability in designed three- and four-stranded beta-sheets.
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Summary
It is suggested that antiparallel beta-sheet does, in general, become more stable when the number of strands is increased from two to three, and this conclusion is not influenced by the rigidity of the loop segment used to link adjacent beta-strands.
- Type
- article
- Published
- 2003-01-30
- Cited by
- 11
- References
- 84
- OpenAlex
- https://openalex.org/W2011433843
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:14109568
Keywords
Antiparallel (mathematics), Beta sheet, Crystallography, BETA (programming language), Chemistry
References
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- A novel, convenient, three-dimensional orthogonal strategy for solid-phase synthesis of cyclic peptides
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- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OH
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- De novo design and structural analysis of a model β-hairpin peptide system
- Stereochemical Requirements for β-Hairpin Formation: Model Studies with Four-Residue Peptides and Depsipeptides
Cited by
- Tetrad selectivity in polarity‐driven switch peptides: the best turn is not always the best nucleation site
- Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies
- Sequence determinants of thermodynamic stability in a WW domain—An all‐β‐sheet protein
- Probing the Nanosecond Dynamics of a Designed Three-Stranded Beta-Sheet with a Massively Parallel Molecular Dynamics Simulation
- Probing the kinetic cooperativity of beta-sheet folding perpendicular to the strand direction.
- Structure‐based design of ferritin nanoparticle immunogens displaying antigenic loops of Neisseria gonorrhoeae
- Analysis of the thermal stability of mercuric reductase from the hot brine environment of Atlantis II in the Red Sea by site-directed mutagenesis: Structural interpretation of thermolabile and enhanced thermostable mutants
- Optimising His-tags for purification and phasing
- Rational design of antibody‐like peptides for targeting the human complement fragment protein C5a
- Thermodynamic Analysis of β‐Sheet Secondary Structure by Backbone Thioester Exchange
- Folding cooperativity in a 3-stranded β-sheet model
- Analysis of the thermal stability of mercuric reductase from the hot brine environment of Atlantis II in the Red Sea by site-directed mutagenesis : Structural interpretation of thermolabile and enhanced thermostable mutants
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