ArticleBiophysical journal2004
Analysis of side-chain rotamers in transmembrane proteins.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- intDesc-AbMut: A Tool for Describing and Understanding How Antibody Mutations Impact Their Environmental Interactions.Computational and structural biotechnology journal · 2026Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Insight Into Pathological Integrin αIIbβ3 Activation From Safeguarding The Inactive State.Journal of molecular biology · 2021Article
- Mapping the functional anatomy of Orai1 transmembrane domains for CRAC channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Membrane Anchoring of α-Helical Proteins: Role of Tryptophan.The journal of physical chemistry. B · 2018Article
- Methods for the Development of In Silico GPCR Models.Methods in enzymology · 2017Article
- Direct Evaluation of Protein-Lipid Contacts Reveals Protein Membrane Immersion and Isotropic Bicelle Structure.The journal of physical chemistry letters · 2016Article
- Strength of a bifurcated H bond.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The power of hard-sphere models: explaining side-chain dihedral angle distributions of Thr and Val.Biophysical journal · 2012Article
- Developing a high-quality scoring function for membrane protein structures based on specific inter-residue interactions.Journal of computer-aided molecular design · 2012Article
- Molecular origin of electron paramagnetic resonance line shapes on β-barrel membrane proteins: the local solvation environment modulates spin-label configuration.Biochemistry · 2011Article
- Membrane protein folding: how important are hydrogen bonds?Current opinion in structural biology · 2011Review
- Structural origins of nitroxide side chain dynamics on membrane protein α-helical sites.Biochemistry · 2010Article
- Orientation and dynamics of transmembrane peptides: the power of simple models.European biophysics journal : EBJ · 2010Review
- RHYTHM--a server to predict the orientation of transmembrane helices in channels and membrane-coils.Nucleic acids research · 2009Article
- Structure of the integrin alphaIIb transmembrane segment.The Journal of biological chemistry · 2008Article
- Is there a preferential interaction between cholesterol and tryptophan residues in membrane proteins?Biochemistry · 2008Article
- Amino-acid solvation structure in transmembrane helices from molecular dynamics simulations.Biophysical journal · 2006Article
- A limited universe of membrane protein families and folds.Protein science : a publication of the Protein Society · 2006Article
- NMR study of the tetrameric KcsA potassium channel in detergent micelles.Protein science : a publication of the Protein Society · 2006Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We measured the frequency of side-chain rotamers in 14 alpha-helical and 16 beta-barrel membrane protein structures and found that the membrane environment considerably perturbs the rotamer frequencies compared to soluble proteins. Although there are limited experimental data, we found statistically significant changes in rotamer preferences depending on the residue environment. Rotamer distributions were influenced by whether the residues were lipid or protein facing, and whether the residues were found near the N- or C-terminus. Hydrogen-bonding interactions with the helical backbone perturbs the rotamer populations of Ser and His. Trp and Tyr favor side-chain conformations that allow their side chains to extend their polar atoms out of the membrane core, thereby aligning the side-chain polarity gradient with the polarity gradient of the membrane. Our results demonstrate how the membrane environment influences protein structures, providing information that will be useful in the structure prediction and design of transmembrane proteins.
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