Ser and Thr Residues Modulate the Conformation of Pro-Kinked Transmembrane α-Helices
- 1 January 2004
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 86 (1) , 105-115
- https://doi.org/10.1016/s0006-3495(04)74088-6
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The G-Protein-Coupled Receptors in the Human Genome Form Five Main Families. Phylogenetic Analysis, Paralogon Groups, and FingerprintsMolecular Pharmacology, 2003
- Proline-induced Distortions of Transmembrane HelicesJournal of Molecular Biology, 2002
- Serine and Threonine Residues Bend α-Helices in the χ1=g− ConformationBiophysical Journal, 2000
- HELANAL: A Program to Characterize Helix Geometry in ProteinsJournal of Biomolecular Structure and Dynamics, 2000
- Uncovering Molecular Mechanisms Involved in Activation of G Protein-Coupled ReceptorsEndocrine Reviews, 2000
- C—H⋯O hydrogen bond involving proline residues in α-helicesJournal of Molecular Biology, 1998
- Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of RhodopsinScience, 1996
- A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic MoleculesJournal of the American Chemical Society, 1995
- [19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptorsPublished by Elsevier ,1995
- Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systemsThe Journal of Chemical Physics, 1993