Influence of Strand Number on Antiparallel β-Sheet Stability in Designed Three- and Four-stranded β-Sheets

Syud, Faisal A.; Stanger, Heather E.; Mortell, Heather Schenck; Espinosa, Juan F.; Fisk, John D.; Fry, Charles G.; Gellman, Samuel H.

doi:10.1016/s0022-2836(02)01304-9

Cited by 55 publications

(77 citation statements)

References 64 publications

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“…The CD of O D PG shows a two-band dichroic profile with a maximum *200 nm (O ¼ 4000) and a minimum at 215 nm (O ¼ À4000) that suggests significant sheet and turn structure in agreement with Gellman's studies (Figure 1, red line). 23 The CD spec- To understand the structural details of these newly designed Aib-turn containing peptides at the atomic level, we carried out NMR spectroscopy in aqueous solutions, focusing on OBG, OB Coupling constants along the backbone of the average solution structure were at most *2 Hz of the experimentally measured constants, with the exception of L11 which precedes the C-terminal residue.…”

Section: Resultsmentioning

confidence: 99%

“…amino acids, [19][20][21][22] and/or they incorporate designed cross-strand side-chain interactions. 11,21,[23][24][25][26][27] A key aspect towards designing stable, nonaggregating bsheets, pioneered by Gellman and coworkers, is how exactly to engineer residues in the i + 1 and i + 2 turn positions so as to confer the proper handedness of a four-residue bturn. 19,28,29 Thus, the so-called ''mirror image'' type I 0 (e.g., proteogenic Asn-Gly) 16,17,30 and type II 0 (e.g., nonproteogenic DPro-Gly) 9,10 turns are compatible with the natural right-handed twist of the sheets.…”

Section: Introductionmentioning

confidence: 99%

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Nonstereogenic α‐aminoisobutyryl‐glycyl dipeptidyl unit nucleates type I′ β‐turn in linear peptides in aqueous solution

et al. 2007

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The use of alpha,alpha-disubstituted amino acids represents a valuable strategy to exercise conformational control in peptides. Incorporation of the nonstereogenic alpha-aminoisobutyryl-glycyl (Aib-Gly) dipeptidyl sequence into i+1 and i+2 positions of an acyclic peptide sequence, originally designed and investigated by Gellman and coworkers, [H-Arg-Tyr-Val-Glu-Val-Yyy-Xxx-Orn-Lys-Ile-Leu-Gln-NH2] nucleates a stable [2:4] left-handed type I' beta-turn in water. NMR spectra show that this newly designed beta-hairpin does not aggregate in water up to a concentration of approximately 1 mM, and that its backbone conformation is superimposable on corresponding hairpins containing the DPro-Gly (literature) and Aib-DAla (this work) sequences. The Aib-Gly turn-inducer sequence eliminates complications because of cis-trans isomerization of Zzz-Pro bonds, and constitutes an attractive alternative to the proteogenic Asn-Gly and nonproteogenic DPro-Gly motifs previously suggested as turn-inducer sequences. These design principles could be exploited to prepare water-soluble beta-hairpin peptides with robust structures and novel function.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Nonstereogenic α‐aminoisobutyryl‐glycyl dipeptidyl unit nucleates type I′ β‐turn in linear peptides in aqueous solution

et al. 2007

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“…1 and 5A). Antiparallel ␤-sheet structures are known to stabilize proteins, especially when the number of strands present is greater than 2 (62). MerA has five ␤-strands within its dimerization domain (48).…”

Section: Discussionmentioning

confidence: 99%

A Novel Mercuric Reductase from the Unique Deep Brine Environment of Atlantis II in the Red Sea

Sayed

Ghazy

Ferreira

et al. 2014

Journal of Biological Chemistry

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Background: Molecular features underlying enzyme function in extreme environments are poorly understood. Results: Identification of the basis for thermostability, halophilicity, and detoxification activity in a mercuric reductase from hot deep-sea brine. Conclusion: A small number of structural modifications accounts for the enzyme's robustness. Significance: This work defines novel adaptations that enable enzymes to cope with multiple abiotic stressors simultaneously.

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“…[2][3][4][5] Designed peptides that populated a -hairpin fold in water were not reported until the 1990s. [6][7][8] Once it became clear that, in some contrast to proteins, peptide hairpin formation requires residues at the turn locus that are particularly favorable for chain direction reversal, notably Asn-Gly, 8-10 D-Pro-Gly (designated as pG throughout), [11][12][13] and Pro-Asp-Gly, 6,14 progress was made in the design of hairpins and a variety of three-stranded [15][16][17][18][19][20][21] and four-stranded 22,23 sheet models. Even with favorable turn residues, measurable peptide hairpin populations in water also require cross-strand hydrophobic clustering 10,24 or aromatic stacking interactions 25,26 and the inclusion of -branched residues in the strands.…”

Section: Introductionmentioning

confidence: 99%

Measuring cooperativity in the formation of a three‐stranded β sheet (double hairpin)

Hudson

Andersen

2006

Biopolymers

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Recently validated chemical shift measures of hairpin structuring have been applied to a series of turn mutants of the Schenck-Gellman three-strand beta-sheet model with the aim of measuring the entropic advantage associated with aligning an additional strand onto an existing hairpin versus aligning the same two strands in an initial hairpin formation. In a four-state analysis (unfolded, 2 single hairpins, and the double hairpin fold in equilibrium) a cooperativity index can be defined as the factor by which the equilibrium constant for hairpin formation is improved when one strand is prestructured. This cooperativity index is 2.7 +/- 0.7 for hairpin formation about a stable D-Pro-Gly turn locus and increases to 7.6 +/- 1.2 for an Asn-Gly turn locus. The latter corresponds to a cooperativity induced DeltaDeltaG increment of 4.9 kJ/mol for the folding of a hairpin. Although larger than previous experimental measures of folding cooperativity in three-stranded sheets, the magnitude of this effect (which is considerably less than the TDeltaDeltaS expectation for prestructuring three or more beta-strand residue sites) likely reflects the intrinsic preference of these designed sequences for extended conformations. If similar or larger effects apply to protein beta-sheet folding, it is not surprising that particularly favorable hairpin alignments serve as nucleation sites in protein folding pathways.

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Influence of Strand Number on Antiparallel β-Sheet Stability in Designed Three- and Four-stranded β-Sheets

Cited by 55 publications

References 64 publications

Nonstereogenic α‐aminoisobutyryl‐glycyl dipeptidyl unit nucleates type I′ β‐turn in linear peptides in aqueous solution

Nonstereogenic α‐aminoisobutyryl‐glycyl dipeptidyl unit nucleates type I′ β‐turn in linear peptides in aqueous solution

A Novel Mercuric Reductase from the Unique Deep Brine Environment of Atlantis II in the Red Sea

Measuring cooperativity in the formation of a three‐stranded β sheet (double hairpin)

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