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Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Folding and Stability.

Journal of the American Chemical Society

Eberhardt ES, Panisik N, Raines RT.
PMID: 21451735
J Am Chem Soc. 1996;118(49):12261-12266. doi: 10.1021/ja9623119.

The hydroxylation of proline residues in collagen enhances the stability of the collagen triple helix. Previous X-ray diffraction analyses had demonstrated that the presence of an electron-withdrawing substituent on the pyrrolidine ring of proline residues has significant structural consequences...

Cite
Eberhardt ES, Panisik N, Raines RT. Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Folding and Stability. J Am Chem Soc. 1996;118(49):12261-12266doi: 10.1021/ja9623119.
Eberhardt, E. S., Panisik, N., & Raines, R. T. (1996). Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Folding and Stability. Journal of the American Chemical Society, 118(49), 12261-12266. https://doi.org/10.1021/ja9623119
Eberhardt, Eric S, et al. "Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Folding and Stability." Journal of the American Chemical Society vol. 118,49 (1996): 12261-12266. doi: https://doi.org/10.1021/ja9623119
Eberhardt ES, Panisik N, Raines RT. Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Folding and Stability. J Am Chem Soc. 1996;118(49):12261-12266. doi: 10.1021/ja9623119. PMID: 21451735; PMCID: PMC3065073.
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Enhanced Protein Thermostability by Ala --> Aib Replacement.

Biochemistry

De Filippis V, De Antoni F, Frigo M, Polverino de Laureto P, Fontana A.
PMID: 9485298
Biochemistry. 1998 Feb 10;37(6):1686-96. doi: 10.1021/bi971937o.

The introduction into peptide chains of alpha-aminoisobutyric acid (Aib) has proven to stabilize the helical structure in short peptides by restricting the available range of polypeptide backbone conformations. In order to evaluate the potential stabilizing effect of Aib at...

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De Filippis V, De Antoni F, Frigo M, et al. Enhanced Protein Thermostability by Ala --> Aib Replacement. Biochemistry. 1998;37(6):1686-96doi: 10.1021/bi971937o.
De Filippis V, De Antoni F, Frigo, M., Polverino de Laureto P, & Fontana, A. (1998). Enhanced Protein Thermostability by Ala --> Aib Replacement. Biochemistry, 37(6), 1686-96. https://doi.org/10.1021/bi971937o
De Filippis V, et al. "Enhanced Protein Thermostability by Ala --> Aib Replacement." Biochemistry vol. 37,6 (1998): 1686-96. doi: https://doi.org/10.1021/bi971937o
De Filippis V, De Antoni F, Frigo M, Polverino de Laureto P, Fontana A. Enhanced Protein Thermostability by Ala --> Aib Replacement. Biochemistry. 1998 Feb 10;37(6):1686-96. doi: 10.1021/bi971937o. PMID: 9485298.
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Issue dedicated to Professor Bruce Merrifield on the occasion of his 70th birthday.

International journal of peptide and protein research

[No authors listed]
PMID: 1478775
Int J Pept Protein Res. 1992 Sep-Oct;40(3):161-349.

No abstract available.

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Issue dedicated to Professor Bruce Merrifield on the occasion of his 70th birthday. Int J Pept Protein Res. 1992;40(3):161-349
(1992). Issue dedicated to Professor Bruce Merrifield on the occasion of his 70th birthday. International journal of peptide and protein research, 40(3), 161-349.
"Issue dedicated to Professor Bruce Merrifield on the occasion of his 70th birthday." International journal of peptide and protein research vol. 40,3 (1992): 161-349.
Issue dedicated to Professor Bruce Merrifield on the occasion of his 70th birthday. Int J Pept Protein Res. 1992 Sep-Oct;40(3):161-349. PMID: 1478775.
Copy Download .nbib Format: NLM
Showing 1 to 3 of 3 entries