Výsledky vyhledávání - "Shao Qing Peng"

Non-linear hydrophobic-induced pKa shifts: Implications for efficiency of conversion to chemical energy

Autor: Timothy M. Parker, D. Channe Gowda, Shao Qing Peng, Dan W. Urry

Publikováno v: Chemical Physics Letters. 239:67-74

By using one Asp or one Glu per thirty residues in a polytricosapeptide capable of exhibiting a hydrophobic folding and assembly transition and stepwise converting a set of the five Val residues (most proximal to the Asp or Glu residue) to more-hydro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::374e65425a1944592b0c6b83c97b9bd6
https://doi.org/10.1016/0009-2614(95)00442-7

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Electrochemical Transduction in Elastic Protein-Based Polymers: A Model for an Energy Conversion Step of Oxidative Phosphorylation

Autor: L. C. Hayes, Naijie Jing, D. C. Gowda, Shao Qing Peng, Dan W. Urry

Publikováno v: Biochemical and Biophysical Research Communications. 210:1031-1039

A pair of functional moieties, the carboxyl of an aspartic acid (Asp, D) residue and an N-methyl nicotinamide (NMeN) formed on amide linkage to the epsilon-amino group of the lysine (Lys, K) residue, are coupled to perform energy conversion by means

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01ad4f5068075f977d46288a483f0a08
https://doi.org/10.1006/bbrc.1995.1760

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Hydrophobicity-induced pK shifts in elastin protein-based polymers

Autor: Timothy M. Parker, Shao Qing Peng, Dan W. Urry

Publikováno v: Biopolymers. 32:373-379

Three polypentapeptides--poly[0.8(GVGVP), 0.2(GEGVP)], poly[0.8(GVGIP), 0.2(GEGIP)], and poly[0.75(GFGVP), 0.25(GEGVP)]--all analogues of the polypentapeptide of elastin--(Val1-Pro2-Gly3-Val4-Gly5)n or poly(VPGVG)--have been prepared to determine the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f535d8d5bf25f155d40d45545e6645b0
https://doi.org/10.1002/bip.360320413

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Molecular Biophysics of Elastin Structure, Function and Pathology

Autor: Dan W. Urry, Shao Qing Peng, Chi Hao Luan

Publikováno v: Ciba Foundation Symposium 192-The Molecular Biology and Pathology of Elastic Tissues

Owing to the presence of the recurring sequence XPGX' (where X and X' are hydrophobic residues), the molecular structure of the sequences between cross-links in elastin is viewed primarily as a series of beta-turns which become helically ordered by h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c0c11a0e5f2ef4c0d11a86781e628bab
https://doi.org/10.1002/9780470514771.ch2

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Designing for advanced materials by the ΔT t -mechanism

Autor: Larry C. Hayes, Shao Qing Peng, Dan W. Urry

Publikováno v: Smart Structures and Materials 1996: Smart Materials Technologies and Biomimetics.

Smart functions in biological systems are discussed from the perspective of the temperature at which inverse transitions of hydrophobic folding and assembly occur in response to increases in the temperature. The design of advanced materials is demons

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d0e1707896f8aed190af57fcee8559b5
https://doi.org/10.1117/12.232162

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Synthesis and characterization of the human elastin W4 sequence

Autor: Naijie Jing, Cynthia M. Harris, R.L. Furner, Chi Hao Luan, Shao Qing Peng, Dan W. Urry, Timothy M. Parker, D. C. Gowda

Publikováno v: International journal of peptide and protein research. 46(6)

Following the nomenclature of Sandberg, the W4 sequence of human elastin, [sequence: see text], has been synthesized by solid-phase methods and characterized by carbon-13 nuclear magnetic resonance, amino-acid analysis, mass spectra and elemental ana

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ba2fa725f6f05f29065c38fe7eb7092
https://pubmed.ncbi.nlm.nih.gov/8748705

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