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  • 1
    Electronic Resource
    Electronic Resource
    Solvent deuteration enhancement of hydrophobicity: DSC study of the inverse temperature transition of elastin-based polypeptides (1991)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 95 (1991), S. 7896-7900 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100173a063
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  • 2
    Electronic Resource
    Electronic Resource
    Dielectric relaxation studies on analogs of the polypentapeptide of elastin (1988)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 92 (1988), S. 511-517 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100313a053
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  • 3
    Electronic Resource
    Electronic Resource
    Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity (1991)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 113 (1991), S. 4346-4348 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00011a057
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  • 4
    Electronic Resource
    Electronic Resource
    Cyclododecapeptide analog of the polyhexapeptide of elastin: 2-D NMR and molecular dynamics studies (1990)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 38 (1990), S. 145-159 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The hexapeptide, (APGVGV), is one of the repeating sequences found in the natural protein, elastin. The cyclododecapeptide, cyclo(L-Ala1-L-Pro2-Gly3-L-Val4-Gly5-L-Val6)2, was synthesized and was found to undergo an inverse temperature transition leading to crystallization. Extensive NMR experiments have been carried out previously to evaluate its secondary structure in comparison to that of its linear counterpart, polyhexapeptide (APGVGV)n, directly and in terms of the concept of cyclic conformations with linear conformational correlates. Building on the previous work, this report adds 2-D NMR and molecular dynamics studies on the molecular structure of the cyclododecapeptide. From the 2-D COSY and 2-D NOESY experimental results, a reversal of the previous Gly3 and Gly5 resonance assignments in the cyclododecapeptide is reported. And in the 2-D NOESY study, a prominent NOE is found between the NH's of the two valine residues at position 4 and 6. Because the Val4 and Val6 residues are not adjacent to each other sequentially, the proximity of these two backbone hydrogens is used as an imposed constraint in constructing the molecular structure of the cyclododecapeptide. Molecular dynamics investigations were employed using the information from the 1-D and 2-D NMR experiments to arrive at potential molecular structures of the cyclododecapeptide. The characteristic secondary structural feature obtained is the expected Type II Pro2-Gly3 β-turn consisting of the 10-membered hydrogen bond between the residue-4 NH and the residue-1 C=O, a feature previously found in this and all other repeating peptides in elastin which contain the Pro2-Gly3 sequence.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560381716
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  • 5
    Electronic Resource
    Electronic Resource
    β-Spiral conformations of the elastomeric polytetrapeptides, (VPGG)n and (IPGG)n, by 2D NMR and molecular mechanics studies (1991)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 40 (1991), S. 183-198 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The synthetic polytetrapeptide using the repeating sequence VPGG found in the fibrous protein, elastin, exhibits a reversible inverse temperature transition, i.e., the molecular order increases on raising the temperature of the polypeptide in aqueous solutions. The matrices formed from the coacervate by γ-irradiation-induced cross-linking exhibit an elastic modulus and temperature dependence of elastomeric force with similarity to that of fibrous elastin. As demonstrated on poly(VPGVG), which forms a β-spiral structure with recurring Type II β-turns, the molecular structure of the elastin-based polypeptides is fundamental to an understanding of the mechanism of elasticity.It was found previously that the repeating unit VPGG in the polytetrapeptide forms a Type II β-turn with a hydrogen bond between Val1 C=O and Gly4 NH. This secondary structural feature is confirmed in this report by 2D NMR data as indicated by specific NOE cross-peaks, particularly, dNN(3,4), dαN(2,3), dαN(2,4), and dγN(1,4). The same secondary structural feature is found in the 2D NMR data for its analog polypeptide, poly(IPGG).The NMR data provide conclusive evidence for the Type II β-turn secondary structure. Molecular mechanics computations were performed to develop a more detailed tertiary structure for the polytetrapeptides. The ECEPP/2 potential field and build-up strategy were employed in mapping conformational space of VPGG and its high polymer. In addition, helical structures are sought using the Go-Scheraga condition, on the assumption that the repeated sequence would preferentially adopt a helical or nearhelical conformation on optimization of intramolecular hydrophobic contacts. A number of structures with helically recurring β-turns was obtained and can be used as starting structures in future studies that are to include hydration. The structures were also evaluated in terms of potential energy using the CHARMm force field.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560400719
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular mechanics study of the β-spiral conformations of the Phe4, Tyr4, and Trp4 analogs of elastomeric poly(Val1-Pro2-Gly3-Val4-Gly5) (1992)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 42 (1992), S. 1439-1448 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The elastin-derived polypentapeptide, poly(VPGVG), and analogs are becoming model systems for protein as well as forming a new class of biomaterials. The β-spiral of poly(VPGVG) represents a new family of molecular structures in fibrous proteins. In particular for our interests here, aromatic amino acid residue substitutions at position four of poly(VPGVG) give rise to new polypeptides with interesting properties of increased elastic modulus, pressure sensitivity, etc. Molecular mechanics computations were carried out to answer the question, can the polypeptides with Phe, Tyr, and Trp substitution at position four of poly(VPGVG) form a β-spiral structure like poly(VPGVG)? Employed in this study was a combination of conformational search using ECEPP/2 and the build-up strategy and of molecular dynamics calculations using CHARMm. The results indicate that the VPGX Type II β-turn structure appears to be the most prominent secondary structural feature for the three aromatic residues containing polypentapeptides, although there is more evidence for VPGFG and VPGVG to assume the VPGVG-type structure than for VPGWG to do so. The study also shows that the aromatic side chains do not interrupt the β-spiral structure, even in the case of tryptophan.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560420519
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  • 7
    Electronic Resource
    Electronic Resource
    Dielectric relaxation studies on bovine ligamentum nuchae (1988)
    New York : Wiley-Blackwell
    Biopolymers 27 (1988), S. 1787-1793 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Dielectric relaxation studies of bovine ligamentum nuchae are reported over the frequency range of 1 MHz to 1 GHz and over the temperature range of 23-48°C. A temperature-dependent relaxation process was observed at low megahertz-frequency with the correlation time of around 40 ns. The result is quite similar to that of a synthetic polypentapeptide (VPGVG) and of α-elastin. The relaxation is proposed to arise in part from the peptide libration within the polypentapeptide of bovine ligamentum nuchae.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360271108
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  • 8
    Electronic Resource
    Electronic Resource
    Differential scanning calorimetry studies of the inverse temperature transition of the polypentapeptide of elastin and its analogues (1990)
    New York : Wiley-Blackwell
    Biopolymers 29 (1990), S. 1699-1706 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Differential scanning calorimetry studies have been carried out on the sequential polypeptide of elastin, (L-Val1-L-Pro2-Gly3-L-Val4-Gly5)n, abrreviated as PPP, and its more hydrophobic analogues (L-Val1-L-Pro2-Gly3-L-Val4-Gly5)n, referred to as Leu1-PPP, and (L-Ile1-L-Pro2-Gly3-L-Val4-Gly5)n, referred to as Ile1-PPP. Consistent with inverse temperature transitions, the temperatures of the transitions for which maximum heat absorption occurs are inversely proportional to the hydrophobicities of the polypentapeptides (31°C for PPP, 16°C for Leu1-PPP, and 12°C for Ile1-PPP), and the endothermic heats of the transitions are small and increase with increasing hydrophobicity, i.e., 1.2, 2.9, and 3.0 kcal/mol pentamer for PPP, Leu1-PPP, and Ile1-PPP, respectively. Previous physical characterizations of the polypentapeptides have demonstrated the occurrence of an inverse temperature transition since increase in order, as the temperature is raised above that of the transition, has been repeatedly observed using different physical characterizations. Furthermore, the studies demonstrated indentical conformations for PPP and Ile1-PPP above and below the transition. Both heats and temperature of the transitions vary with hydrophobicity, but not in simple proportionality.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360291403
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  • 9
    Electronic Resource
    Electronic Resource
    Hydrophobicity scale for proteins based on inverse temperature transitions (1992)
    New York : Wiley-Blackwell
    Biopolymers 32 (1992), S. 1243-1250 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In general, proteins fold with hydrophobia residues buried, away from water. Reversible protein folding due to hydrophobia interactions results from inverse temperature transitions where folding occurs on raising the temperature. Because homoiothermic animals constitute an infinite heat reservoir, it is the transition temperature, Tt, not the endothermic heat of the transition, that determines the hydrophobically folded state of polypeptides at body temperature. Reported here is a new hydrophobicity scale based on the values of Tt for each amino acid residue as a guest in a natural repeating peptide sequence, the high polymers of which exhibit reversible inverse temperature transitions. Significantly, a number of ways have been demonstrated for changing Tt such that reversibly lowering Tt, from above to below physiological temperature becomes a means of isothermally and reversibly driving hydrophobic folding. Accordingly, controlling Tt, becomes a mechanism whereby proteins can be induced to carry out isothermal free energy transduction. © 1992 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360320913
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  • 10
    Electronic Resource
    Electronic Resource
    Differential scanning calorimetry studies of NaCl effect on the inverse temperature transition of some elastin-based polytetra-, polypenta-, and polynonapeptides (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 465-475 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Differential scanning calorimetry studies of the effect of NaCl on protein-based polymer self-assembly has been carried out on six elastin-based synthetic sequential polypeptides- i.e., the polypentapeptide (L-Val1-L-Pro2-Gly3-L-Val4-Gly5)n and its more hydrophobic analogues (L-Leu1-L-Pro2-Gly3-L-Val4-Gly5)n and (L-Val1-L-Pro2-L-Ala3-L-Val4-Gly5)n; the polytetrapeptide (L-Val1-L-Pro2-Gly3-Gly4)n and its more hydrophobic analogue (L-IIe1-L-Pro2-Gly3-Gly4)n; and the polynonapeptide (a pentatetra hybrid), (L-Val1-L-Pro2-Gly3-L-Val4-Gly5-L-Val6-L-Pro7-Gly8-Gly9)n.Previous physical characterizations of the polypentapeptides have demonstrated the occurrence of an inverse temperature transition since increase in order of the polypentapeptide, as the temperature is raised from below to above that of the transition, has been repeatedly observed using different physical characterizations.In the present experiments, it is observed that the transition temperatures of the polypeptides studied are linearly dependent on NaCl concentration. The molar effectiveness of NaCl in shifting the transition temperature ΔTm/[N], is about 14°C/[N], with the dependence on peptide hydrophobicity being fairly small. Interestingly, however, the δΔQ/ [N] does depend on the hydrophobicity of a polypeptide.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310502
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