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Literature DB >> 19919159

Hydrogen bonding of beta-turn structure is stabilized in D(2)O.

Younhee Cho¹, Laura B Sagle, Satoshi Iimura, Yanjie Zhang, Jaibir Kherb, Ashutosh Chilkoti, J Martin Scholtz, Paul S Cremer.

Abstract

The lower critical solution temperature (LCST) of elastin-like polypeptides (ELPs) was investigated as a function of ELP chain length and guest residue chemistry. These measurements were made in both D(2)O and H(2)O. Differences in the LCST values with heavy and light water were correlated with secondary structure formation of the polypeptide chains. Such structural information was obtained by circular dichroism and infrared measurements. Additional thermodynamic data were obtained by differential scanning calorimetry. It was found that there is a greater change in the LCST value between H(2)O and D(2)O for those polypeptides which form the greatest amount of beta-turn/beta-aggregate structure. Moreover, these same molecules were the least hydrophobic ELPs. Therefore, hydrogen bonding rather than hydrophobicity was the key factor in the stabilization of the collapsed state of ELPs in D(2)O compared with H(2)O.

Entities: Chemical Disease Gene Species

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Year: 2009 PMID： 19919159 PMCID： PMC3003597 DOI： 10.1021/ja9040785

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

49 in total

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5. The effect of D2-O on the thermal stability of proteins. Thermodynamic parameters for the transfer of model compounds from H2-O to D2-O.

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10. Molecular dynamics of hydrogen bonds in protein-D2O: the solvent isotope effect.

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Review 10. Application of Thermoresponsive Intrinsically Disordered Protein Polymers in Nanostructured and Microstructured Materials.

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Hydrogen bonding of beta-turn structure is stabilized in D(2)O.

1. Reusable platforms for high-throughput on-chip temperature gradient assays.

2. Mechanism for the phase transition of a genetically engineered elastin model peptide (VPGIG)40 in aqueous solution.

3. An infrared spectroscopic study of the conformational transition of elastin-like polypeptides.

4. Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, deltaH(o), deltaS(o), and deltaC(o)p and evaluation of solvent isotope effects.

5. The effect of D2-O on the thermal stability of proteins. Thermodynamic parameters for the transfer of model compounds from H2-O to D2-O.

6. Aqueous two-phase system formation kinetics for elastin-like polypeptides of varying chain length.

Review 7. Hydrogen bonding in globular proteins.

8. Interfacial phase transition of an environmentally responsive elastin biopolymer adsorbed on functionalized gold nanoparticles studied by colloidal surface plasmon resonance.

9. Bovine elastin and kappa-elastin secondary structure determination by optical spectroscopies.

10. Molecular dynamics of hydrogen bonds in protein-D2O: the solvent isotope effect.

1. Fractal dimension of an intrinsically disordered protein: small-angle X-ray scattering and computational study of the bacteriophage λ N protein.

2. Designer amphiphilic proteins as building blocks for the intracellular formation of organelle-like compartments.

3. Injectable tissue integrating networks from recombinant polypeptides with tunable order.

4. Deuterium induces a distinctive Escherichia coli proteome that correlates with the reduction in growth rate.

5. Isotopically induced variation in the stability of FMN-wrapped carbon nanotubes.

6. A large solvent isotope effect on protein association thermodynamics.

7. Multifunctional elastin-like polypeptide renders β-glucosidase enzyme phase transition and high stability.

8. A new criterion to evaluate water vapor interference in protein secondary structural analysis by FTIR spectroscopy.

9. Guanidinium can both Cause and Prevent the Hydrophobic Collapse of Biomacromolecules.

Review 10. Application of Thermoresponsive Intrinsically Disordered Protein Polymers in Nanostructured and Microstructured Materials.