𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Hydrophobicity and amphiphilicity in protein structure

✍ Scribed by David Eisenberg; William Wilcox; Andrew D. McLachlan

Publisher
John Wiley and Sons
Year
1986
Tongue
English
Weight
357 KB
Volume
31
Category
Article
ISSN
0730-2312

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Local hydrophobicity stabilizes secondar
Local hydrophobicity stabilizes secondary structures in proteins
✍ Minoru I. Kanehisa; Tian Yow Tsong 📂 Article 📅 1980 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 661 KB

## Abstract The probability of occurrence of helix and β‐sheet residues in 47 globular proteins was determined as a function of local hydrophobicity, which was defined by the sum of the Nozaki‐Tanford transfer free energies at two nearest‐neighbors on both sides of the amino acid sequence. In gener

Solvent structure at a hydrophobic prote
Solvent structure at a hydrophobic protein surface
✍ Helena Kovacs; Alan E. Mark; Wilfred F. van Gunsteren 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 228 KB

The impact of an extensive, uniform and hydrophobic protein surface on the behavior of the surrounding solvent is investigated. In particular, focus is placed on the possible enhancement of the structure of water at the interface, one model for the hydrophobic effect. Solvent residence times and rad

Structural characterization of ordered d
Structural characterization of ordered domains in a hydrophobic membrane protein
✍ E. M. Macchi; F. J. Barrantes 📂 Article 📅 1979 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 836 KB

## Abstract A delipidized proteolipid protein fraction was purified from organic solvent extracts of bovine cerebral cortex and studied by means of diffraction, electron microscopic, and ir techniques. Special use was made of an electron diffraction procedure which minimized the electron damage to

Hydrophobic patches on the surfaces of p
Hydrophobic patches on the surfaces of protein structures
✍ Philip Lijnzaad; Herman J. C. Berendsen; Patrick Argos 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 689 KB

A survey of hydrophobic patches on the surface of 112 soluble, monomeric proteins is presented. The largest patch on each individual protein averages around 400 A2 but can range from 200 to 1,200 A2. These areas are not correlated to the sizes of the proteins and only weakly to their apolar surface

Hydrophobicity-induced pK shifts in elas
Hydrophobicity-induced pK shifts in elastin protein-based polymers
✍ Dan W. Urry; Shao Qing Peng; Timothy M. Parker 📂 Article 📅 1992 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 522 KB

## Abstract 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 polypenta‐peptide of elastin—(Val^1^‐Pro^2^‐Gly^3^‐Val^4^‐Gly^5^)~__n__~ or poly(VPGVG)—have been prepared to determine the effect of changing the

Contribution of protein hydrophobicity t
Contribution of protein hydrophobicity to its functionality
✍ Nakai, S. ;Li-Chan, E. ;Hayakawa, S. 📂 Article 📅 1986 🏛 John Wiley and Sons 🌐 English ⚖ 534 KB

HANSCH analysis for quantitative structure-activity relationship (QSAR) was applied to aspartyl proteinases and it was found that higher hydrophobicity, tighter molecular structure, and lower charge are required for milk clotting enzymes compared to proteolytic enzymes. For simplicity in analysis of