Role of different β‐turns in β‐hairpin conformation and stability studied by optical spectroscopy

@article{Wu2012RoleOD,
  title={Role of different $\beta$‐turns in $\beta$‐hairpin conformation and stability studied by optical spectroscopy},
  author={Ling Wu and Dan McElheny and Vladim{\'i}r Setni{\vc}ka and Jovencio Hilario and Timothy A. Keiderling},
  journal={Proteins: Structure},
  year={2012},
  volume={80}
}
Model β‐hairpin peptides based on variations in the turn sequence of Cochran's tryptophan zipper peptide, SWTWENGKWTWK, were studied using electronic circular dichroism (ECD), fluorescence, and infrared (IR) spectroscopies. The trpzip2 Asn–Gly turn sequence was substituted with Thr–Gly, Aib–Gly, DPro–Gly, and Gly–Asn (trpzip1) to study the impact of turn stability on β‐hairpin formation. Stability and conformational changes of these hairpins were monitored by thermodynamic analyses of the… Expand
Impact of β-Turn Sequence on β-Hairpin Dynamics Studied with Infrared-Detected Temperature Jump
Folding dynamics for β-structure loss and disordered structure gain were studied in a model β-hairpin peptide based on Cochran’s tryptophan zipper peptide Trpzip2, but with an altered Thr-Gly (TG)Expand
Effect of hydrophobic interactions on the folding mechanism of β-hairpins.
TLDR
The dynamics of hydrophobic interactions of β-hairpin variants of the sequence Trpzip2 that is stabilized by two cross-strand Trp-Trp pairs are studied using time-resolved infrared spectroscopy to reveal that hydrophobia interactions alone weakly stabilize the hairpin structure, but adding edge-to-face aromatic interaction strengthens it, and both modify the complex folding process. Expand
Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide
TLDR
A possible mechanism is proposed: B3D forms a low‐temperature oligomer, which is at least partially unfolded by heat and subsequently reassembles more slowly as a fibril. Expand
Site-Specific Dynamics of β-Sheet Peptides with (D) Pro-Gly Turns Probed by Laser-Excited Temperature-Jump Infrared Spectroscopy.
TLDR
The relative importance of the turn versus the intrastrand stability in β-sheet formation is discussed and the Xxx-(D) Pro tertiary amide provides a detectable IR band, allowing us to probe the dynamics site-specifically. Expand
Design of monomeric water-soluble β-hairpin and β-sheet peptides.
  • M. Jiménez
  • Chemistry, Medicine
  • Methods in molecular biology
  • 2014
TLDR
This chapter provides an overview of the reported β-hairpin/β-sheet peptides focussed on the applied design criteria, reviews briefly the factors contributing to β- hairpin/ β-sheet stability, and describes a protocol for the de novo design of β-sheets-forming peptides based on them. Expand
Antimicrobial activity and membrane-active mechanism of tryptophan zipper-like β-hairpin antimicrobial peptides
TLDR
The application potential of the designed peptides as promising antimicrobial agents for the control of infectious diseases is revealed and new insights are provided into the design and optimization of highly stable β-hairpin AMPs with great antimicrobial activities and cell selectivities. Expand
Nature of aryl-tyrosine interactions contribute to β-hairpin scaffold stability: NMR evidence for alternate ring geometry.
TLDR
Solution NMR analysis in near-apolar environments suggests the energetically favourable mode of interaction to be T-shaped face-to-edge (FtE) and that a Trp-Tyr interacting pair is the most stabilizing. Expand
Thermodynamic and Structural Impact of α,α-Dialkylated Residue Incorporation in a β-Hairpin Peptide.
TLDR
The results of these experiments show that α,α-dialkylated α-amino acids with side-chain lengths longer than one carbon unit are tolerated in a β-hairpin, although at a moderate cost to folded stability. Expand
Temperature dependence of C-terminal carboxylic group IR absorptions in the amide I' region.
TLDR
General rules for modeling the α-carboxylic IR absorption bands in peptides and proteins as the function of temperature are proposed. Expand
Nascent Hairpins in Proteins: Identifying Turn Loci and Quantitating Turn Contributions to Hairpin Stability.
TLDR
These studies indicate that aryl residues immediately flanking a turn sequence can alter relative turn propensities by as much as 9-11 kJ/mol and will need to be a part of any nascent hairpin recognition algorithm. Expand
...
1
2
3
...

References

SHOWING 1-10 OF 102 REFERENCES
Role of tryptophan-tryptophan interactions in Trpzip beta-hairpin formation, structure, and stability.
TLDR
A series of beta-hairpin peptides based on variations of the TrpZip2 sequence, SWTWENGKWTWK, of Cochran and co-workers were studied using electronic circular dichroism (CD) and infrared (IR) spectra by varying temperature and pH to test the impact of specific Trp interactions on hairpin stability. Expand
Relationship between hydrophobic interactions and secondary structure stability for Trpzip beta-hairpin peptides.
TLDR
Comparison of conformational transitions monitored by CD and IR reveals them to have multistate behavior in which the temperature-induced disruption of the Trp-Trp interaction (tertiary structure) occurs at a lower temperature than the unfolding of the secondary structure. Expand
Turn stability in β‐hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns
TLDR
Experimental measurements in the bhpW context are a useful way to evaluate turn stability for use in protein design projects, and these scaffolds are capable of displaying a diverse set of turns, which can be exploited for the mimicry of protein loops or for generating libraries of reverse turns. Expand
Analysis of the factors that stabilize a designed two‐stranded antiparallel β‐sheet
TLDR
The enthalpic favorability of folding in these designed β‐hairpins suggests that they are excellent scaffolds for studying the fundamental mechanisms by which amino acid sidechains interact with one another in folded proteins. Expand
Effects of turn residues in directing the formation of the β‐sheet and in the stability of the β‐sheet
The designed peptide (denoted 20‐mer, sequence VFITSDPGKTYTEVDPGOKILQ) has been shown to form a three‐strand antiparallel β‐sheet. It is generally believed that the DPro‐Gly segment has theExpand
Understanding the key factors that control the rate of β-hairpin folding
Both turn sequence and interstrand hydrophobic side-chain–side-chain interaction have been suggested to be important determinants of β-hairpin stability. However, their roles in controlling theExpand
Tuning the β‐turn segment in designed peptide β‐hairpins: Construction of a stable type I′ β‐turn nucleus and hairpin–helix transition promoting segments
Designed octapeptides Boc-Leu-Val-Val-Aib-$^DXxx$-Leu-Val-Val-OMe $(^DXxx=^DAla, 3a; ^DVal, 3c$ and $^DPro, 5a)$ and Boc-Leu-Phe-Val-Aib-$^DAla$-Leu-Phe-Val-OMe (3b) have been investigated toExpand
Optical spectroscopic investigations of model beta-sheet hairpins in aqueous solution.
TLDR
Optical spectroscopic data is reported on a series of designed beta hairpins previously shown by NMR to contain a substantial population of beta-sheet structure that contain a designed hydrophobic cluster and a (D)Pro-Gly sequence to promote formation of a turn geometry. Expand
Origin of β-Hairpin Stability in Solution: Structural and Thermodynamic Analysis of the Folding of a Model Peptide Supports Hydrophobic Stabilization in Water
The origin of the stability of isolated β-hairpins in aqueous solution is unclear with contrasting opinions as to the relative importance of interstrand hydrogen bonding, hydrophobic interactions,Expand
Cross-strand coupling and site-specific unfolding thermodynamics of a trpzip beta-hairpin peptide using 13C isotopic labeling and IR spectroscopy.
TLDR
This study illustrates the consequences of multistate conformational change at the residue- or sequence-specific level in a system whose structure is dominated by hydrophobic collapse. Expand
...
1
2
3
4
5
...