✦ LIBER ✦

Protein structure in anisotropic environments: Development of orientational constraints

✍ Scribed by Cross, T. A. ;Quine, J. R.

Publisher: John Wiley and Sons
Year: 2000
Tongue: English
Weight: 246 KB
Volume: 12
Category: Article
ISSN: 1043-7347
DOI: 10.1002/(sici)1099-0534(2000)12:2<55::aid-cmr1>3.0.co;2-k

No coin nor oath required. For personal study only.

✦ Synopsis

Solid state nuclear magnetic resonance has the potential to characterize membrane protein structures at very high resolution. This paper focuses on the use of orientational constraints for this purpose. These constraints are based on observing the orientation dependence of nuclear spin interactions. The interpretation of these observations is based on accurate knowledge of the spin interaction tensors -the tensor element magnitudes and their orientation to the molecular frame. Numerous possibilities exist for developing these orientational constraints, each with their own strengths and weaknesses. This first of two papers focuses on the observation of these constraints and their inherent error, while the second paper demonstrates the utility, advantages, and disadvantages of these constraints for solving protein backbone structure.

📜 SIMILAR VOLUMES

Protein structure in anisotropic environ

Protein structure in anisotropic environments: Unique structural fold from orientational constraints

✍ Quine, J. R. ;Cross, T. A. 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 191 KB 👁 1 views

The mathematical foundation of the determination of protein structure from orientational constraints is described. The tools used are vector algebra, gram matrices, and determinants. The discussion begins in the general abstract setting and proceeds to a discussion of how the methods can be applied

Productivity analysis of object-oriented

Productivity analysis of object-oriented software developed in a commercial environment

✍ Thomas E. Potok; Mladen Vouk; Andy Rindos 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 316 KB 👁 2 views

The introduction of object-oriented technology does not appear to hinder overall productivity on new large commercial projects, but nor does it seem to improve it in the first two product generations. In practice, the governing influence may be the business workflow, and not the methodology.

Development of home orientation in offsp

Development of home orientation in offspring of protein-restricted cats

✍ Patricia Vetula Gallo; Jack Werboff; Kirvin Knox 📂 Article 📅 1984 🏛 John Wiley and Sons 🌐 English ⚖ 851 KB

Structure investigation of amphiphilic c

Structure investigation of amphiphilic cyclopeptides in isotropic and anisotropic environments—a model study simulating peptide–membrane interactions

✍ Marcus Koppitz; Barbara Mathä; Horst Kessler 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 903 KB

It has been proposed that the membrane allows a much more efficient binding of certain small or medium-sized amphiphilic messenger molecules to their receptor, not only by accumulation of the drug, but also by induction of orientations and conformations that are much more favorable for receptor dock

Conformational constraints of tyrosine i

Conformational constraints of tyrosine in protein tyrosine kinase substrates: Information about preferred bioactive side-chain orientation

✍ Paolo Ruzza; Andrea Calderan; Arianna Donella-Deana; Barbara Biondi; Luca Cesaro 📂 Article 📅 2003 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 139 KB

## Abstract The side‐chain orientation of a tyrosine residue located in a peptide, which is an excellent substrate of Syk tyrosine kinase (A. M. Brunati, A. Donella‐Deana, M. Ruzzene, O. Marin, L. A. Pinna, FEBS Letters, 1995, Vol. 367, pp. 149–152), was fixed in the gauche (+) or gauche (−) confor

Structure, dynamics, and topological ori

Structure, dynamics, and topological orientation of the polyether, ionophore antibiotic monensin, in a micellar environment

✍ Eduardo Mercurio; Maria Pellegrini; Dale F. Mierke 📂 Article 📅 1997 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 212 KB 👁 2 views

The structure and dynamics of the ionophoric antibiotic monensin in the presence of micelles have been determined. The conformation of monensin was derived from 50 nuclear Overhauser enhancement (NOE) derived distance restraints and metric-matrix based distance geometry calculations. The conformatio