ReviewFEBS letters2014
Forces stabilizing proteins.
Review in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.
What it found
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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.
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Who cites it
134 citing papers in PubMed.
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- Development of a Composite Pork Quality Index from Instrumental Traits and Its Hyperspectral Prediction.Foods (Basel, Switzerland) · 2026Article
- Enzyme-Inspired Design of Redox-Active Molecules for Promotion of Oxidative Protein Folding.Chembiochem : a European journal of chemical biology · 2026Review
- London Dispersion Governs Stereochemistry, Stability, and Self-Sorting in a System of MJournal of the American Chemical Society · 2026Article
- Accurate protein stability prediction for small domains using mega-scale experiments.bioRxiv : the preprint server for biology · 2026Article
- Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
- Identification and comprehensive characterization of the OVATE family protein in litchi.BMC plant biology · 2026Article
- Impact of acetic acid chromoendoscopy on detection of serrated lesions in the proximal colon compared with white-light endoscopy.Endoscopy international open · 2026Article
- Enzymatic Synthesis of β-lactam Antibiotics: From Enzyme Dataset Construction to Action Mechanism and Semi-Rational Design.Current protein & peptide science · 2026Review
- Resolving Molecular Interactions in Protein Folding Trajectories with NCIPLOT.Journal of chemical information and modeling · 2025Article
- Network Dynamics as Fingerprints of Thermostability in an In Silico-Engineered DyP-Type Peroxidase.ACS catalysis · 2025Article
- Changes in the Aqueous Solvent do not Impact the Internal Ring-Flip Dynamic of Fully Buried F52 in Protein GB1.Chembiochem : a European journal of chemical biology · 2025Article
- Article
- A Multicomponent Reaction-Based Platform Opens New Avenues in Aryl Hydrocarbon Receptor Modulation.ACS central science · 2025Article
- Comparative structural insights and functional analysis for the distinct unbound states of Human AGO proteins.Scientific reports · 2025Article
- Article
- Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function.Trends in biochemical sciences · 2025Review
- Exploring Bovine Serum Albumin (BSA) as a Facile Substrate for Testing of Osmolytes as Cosmetic Ingredients.Molecules (Basel, Switzerland) · 2025Article
74 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
3 authors.
Funding
Abstract
The goal of this article is to summarize what has been learned about the major forces stabilizing proteins since the late 1980s when site-directed mutagenesis became possible. The following conclusions are derived from experimental studies of hydrophobic and hydrogen bonding variants. (1) Based on studies of 138 hydrophobic interaction variants in 11 proteins, burying a -CH2- group on folding contributes 1.1±0.5 kcal/mol to protein stability. (2) The burial of non-polar side chains contributes to protein stability in two ways: first, a term that depends on the removal of the side chains from water and, more importantly, the enhanced London dispersion forces that result from the tight packing in the protein interior. (3) Based on studies of 151 hydrogen bonding variants in 15 proteins, forming a hydrogen bond on folding contributes 1.1±0.8 kcal/mol to protein stability. (4) The contribution of hydrogen bonds to protein stability is strongly context dependent. (5) Hydrogen bonds by side chains and peptide groups make similar contributions to protein stability. (6) Polar group burial can make a favorable contribution to protein stability even if the polar group is not hydrogen bonded. (7) Hydrophobic interactions and hydrogen bonds both make large contributions to protein stability.
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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.