ReviewCurrent opinion in structural biology2011
Membrane protein folding: how important are hydrogen bonds?
Review in Current opinion in structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
77 citing papers in PubMed, 167 citations in OpenAlex.
- Human Endothelial Membrane as a Structural Prototype: A Comparative Analysis withInternational journal of molecular sciences · 2026Article
- Going Deep into the Surface Chemistry of Carbon Dots: Influence of Functional Groups on the Redox Abilities.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Kcnq2 R213 knock-in mice reveal variant- and region-specific mechanisms underlying self-limited familial neonatal-infantile epilepsy and early infantile developmental and epileptic encephalopathy.Acta neuropathologica communications · 2026Article
- Article
- Two novel TMEM67 variations in a Chinese family with recurrent pregnancy loss: a case report.BMC medical genomics · 2024Article
- Deep transfer learning for inter-chain contact predictions of transmembrane protein complexes.Nature communications · 2023Article
- Comparison of Integrin αIIbβ3 Transmembrane Association in Vesicles and Bicelles.Biochemistry · 2023Article
- Chain-Length-Dependent Hydrogen-Bonded Self-Assembly of Terminally Functionalized Discrete Polyketones.Precision chemistry · 2023Article
- Micro-simulation insights into the functional and mechanistic understanding of glycyrrhizin against asthma.Frontiers in pharmacology · 2023Article
- A new glimpse on the active site of SARS-CoV-2 3CLpro, coupled with drug repurposing study.Molecular diversity · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Expanding the Scope of Metastable Species in Hydrogen Bonding-Directed Supramolecular Polymerization.Angewandte Chemie (International ed. in English) · 2022Article
- Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis.Science advances · 2022Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Refining the Phenotypic Spectrum ofFrontiers in pediatrics · 2022Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- Conformational Clamping by a Membrane Ligand Activates the EphA2 Receptor.Journal of molecular biology · 2021Article
- Physicochemical Features and Peculiarities of Interaction of AMP with the Membrane.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?Accounts of chemical research · 2021Review
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Water is an inhospitable environment for protein hydrogen bonds because it is polarizable and capable of forming competitive hydrogen bonds. In contrast, the apolar core of a biological membrane seems like an ideal environment for hydrogen bonds, and it has long been assumed that hydrogen bonding should be a powerful force driving membrane protein folding. Nevertheless, while backbone hydrogen bonds may be much stronger in membrane proteins, experimental measurements indicate that side chain hydrogen bond strengths are not strikingly different in membrane and water soluble proteins. How is this possible? I argue that model compounds in apolar solvents do not adequately describe the system because the protein itself is ignored. The protein chain provides a rich source of competitive hydrogen bonds and a polarizable environment that can weaken hydrogen bonds. Thus, just like water soluble proteins, evolution can drive the creation of potent hydrogen bonds in membrane proteins where necessary, but mitigating forces in their environment must still be overcome.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.