Resolved Fluorescence of the Two Tryptophan Residues in Horse Apomyoglobin

Glandières, Jean-Marie; Twist, Charles; Haouz, Ahmed; Zentz, Christian; Alpert, Bernard

doi:10.1562/0031-8655(2000)071<0382:rfottt>2.0.co;2

Cited by 22 publications

(21 citation statements)

References 29 publications

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“…The quantum efficiency of the two tryptophans in apoMb mutants is very similar and their contributions to the total protein emission appear to be rather additive. This result corroborates previous experimental observations showing that the microenvironments of the two tryptophanyl residues are physically distinct although very close in the primary sequence 15, 16, 19, 20…”

Section: Resultssupporting

confidence: 92%

“…Residue W7 is more exposed to solvent and experiences multiple environments during its fluorescence lifetime. By contrast, W14 is more buried within the protein matrix and its environment is highly rigid 13–16. We previously showed that single point mutations at position 7 or 14, consisting of the replacement of tryptophan with phenylalanine, do not affect the correct fold of this protein whereas the simultaneous substitution of both residues causes incorrect folding with a subsequent loss of heme binding and amyloid fibril formation under native conditions 17, 18.…”

Section: Introductionmentioning

confidence: 99%

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Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain

2003

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The solvent accessibilities to the tryptophanyl microenvironments of wild type sperm whale apomyoglobin (apoMb) and two mutants (W7F and W14F) containing a single tryptophan are measured by fluorescence quenching studies. The results are compared to those relative to horse apoMb. In the wild type sperm whale protein, no difference is noticed in the solvent accessibility of the two indole residues, as documented by the values of the Stern-Volmer constants. By contrast, the two tryptophan residues of horse apoMb are exposed to the solvent in a different way, thus indicating that some local conformational differences exist between the two homologous proteins in solution. The single W --> F substitution at either position 7 or 14 determines local conformational changes that increase the accessibility of the remaining indole residue but do not affect the overall architecture of the protein molecule.

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Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain

2003

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“…Hydrophobic interactions established among non-polar amino acids ensure the stability of globular proteins in solution by shielding the non-polar amino acids in hydrophobic cores, away from the aqueous environment31. In experimental studies, hydration of the hydrophobic core during protein unfolding and hydrophobic collapse during the start of protein folding are frequently monitored using UV fluorescence spectroscopy912323334353637. This spectroscopy technique exploits the intrinsic fluorescence property of proteins to provide sensitive indications of variation in the solvent accessibility of the hydrophobic core caused by changes in tertiary structure32333435.…”

Section: Resultsmentioning

confidence: 99%

“…In the case of apoMb, information with regard to structural changes during folding and unfolding is acquired by monitoring the fluctuations in the fluorescence emission of Trp7 and Trp14, both of which are components of the hydrophobic core of apoMb which are confined by Helices A, G and H (Fig. 4A)123233343538.…”

Section: Resultsmentioning

confidence: 99%

“…As the simulations were adequately conducted to monitor early unfolding of apoMb, only the SASA of Trp7 was measured as this residue is closer to the protein surface and fluctuations in SASA acquired will be more substantial compared to Trp14 which will remain embedded in the hydrophobic core during the course of the simulation (Fig. 4A)32333435. The distribution curves related to the SASA of Trp7 for all four variants were also depicted in Fig.…”

Section: Resultsmentioning

confidence: 99%

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Application of conventional molecular dynamics simulation in evaluating the stability of apomyoglobin in urea solution

Zhang

Lazim

2017

Sci Rep

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In this study, we had exploited the advancement in computer technology to determine the stability of four apomyoglobin variants namely wild type, E109A, E109G and G65A/G73A by conducting conventional molecular dynamics simulations in explicit urea solution. Variations in RMSD, native contacts and solvent accessible surface area of the apomyoglobin variants during the simulation were calculated to probe the effect of mutation on the overall conformation of the protein. Subsequently, the mechanism leading to the destabilization of the apoMb variants was studied through the calculation of correlation matrix, principal component analyses, hydrogen bond analyses and RMSF. The results obtained here correlate well with the study conducted by Baldwin and Luo which showed improved stability of apomyoglobin with E109A mutation and contrariwise for E109G and G65A/G73A mutation. These positive observations showcase the feasibility of exploiting MD simulation in determining protein stability prior to protein expression.

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Transition Metal Ion–Mediated Tyrosine‐Based Short‐Peptide Amphiphile Nanostructures Inhibit Bacterial Growth

et al. 2018

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We report the design and synthesis of a biocompatible small-peptide-based compound for the controlled and targeted delivery of encapsulated bioactive metal ions through transformation of the internal nanostructures of its complexes. A tyrosine-based short-peptide amphiphile (sPA) was synthesized and observed to self-assemble into β-sheet-like secondary structures. The self-assembly of the designed sPA was modulated by application of different bioactive transition-metal ions, as was confirmed by spectroscopic and microscopic techniques. These bioactive metal-ion-conjugated sPA hybrid structures were further used to develop antibacterial materials. As a result of the excellent antibacterial activity of zinc ions the growth of clinically relevant bacteria such as Escherichia coli was inhibited in the presence of zinc⋅sPA conjugate. Bacterial testing demonstrated that, due to high biocompatibility with bacterial cells, the designed sPA acted as a metal ion delivery agent and might therefore show great potential in locally addressing bacterial infections.

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Resolved Fluorescence of the Two Tryptophan Residues in Horse Apomyoglobin

Cited by 22 publications

References 29 publications

Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain

Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain

Application of conventional molecular dynamics simulation in evaluating the stability of apomyoglobin in urea solution

Transition Metal Ion–Mediated Tyrosine‐Based Short‐Peptide Amphiphile Nanostructures Inhibit Bacterial Growth

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