ReviewBiopolymers2008
Roles of beta-turns in protein folding: from peptide models to protein engineering.
Review in Biopolymers, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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.
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.
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Who cites it
78 citing papers in PubMed, 248 citations in OpenAlex.
- A bireporter recombinant SARS-CoV-2 Omicron BA.5 forMicrobiology spectrum · 2026Article
- Enhancement of gel properties of low-salt Scomberomorus niphonius surimi by egg white protein: Structural refinement and intermolecular interaction analysis.Journal of the science of food and agriculture · 2026Article
- Novel polymorphisms and functional characterization of the prion protein gene in sparrows (Frontiers in veterinary science · 2026Article
- A scalable equivariant graph network framework for precise protein function prediction.Genome biology · 2025Article
- Turn-engineering tunes the conformational rigidity of β-hairpin AMPs in achieving membrane selectivity and killing drug-resistant ESKAPE pathogens.Chemical science · 2025Article
- Binding Capacity and Adsorption Stability of Uremic Metabolites to Albumin-Modified Magnetic Nanoparticles.International journal of molecular sciences · 2025Article
- On the stability of acid-soluble pea protein-stabilized beverage emulsions against salt addition and heat treatment.RSC advances · 2025Article
- Mannose-Glycated Metal-Phenolic Microcapsules Orchestrate Phenotype Switch of Macrophages for Boosting Tumor Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- ExploreTurns: A web tool for the exploration, analysis, and classification of beta turns and structured loops in proteins; application to beta-bulge and Schellman loops, Asx helix caps, beta hairpins, and other hydrogen-bonded motifs.Protein science : a publication of the Protein Society · 2025Article
- Protein-Based Degraders: From Chemical Biology Tools to Neo-Therapeutics.Chemical reviews · 2025Review
- Exploring force-driven stochastic folding dynamics in mechano-responsive proteins and implications in phenotypic variation.Nature communications · 2025Article
- DiMA: sequence diversity dynamics analyser for viruses.Briefings in bioinformatics · 2024Article
- Atomistic simulations reveal impacts of missense mutations on the structure and function of SynGAP1.Briefings in bioinformatics · 2024Article
- De novo design of buttressed loops for sculpting protein functions.Nature chemical biology · 2024Article
- AggreProt: a web server for predicting and engineering aggregation prone regions in proteins.Nucleic acids research · 2024Article
- Effect of Organic Solvents on the Activity, Stability and Secondary Structure of asclepain cI, Using FTIR and Molecular Dynamics Simulations.The protein journal · 2024Article
- Spatiotemporal Optical Control of Gαq-PLCβ Interactions.ACS synthetic biology · 2024Article
- Article
- A biallelic variant of DCAF13 implicated in a neuromuscular disorder in humans.European journal of human genetics : EJHG · 2023Article
- Water stabilizes an alternate turn conformation in horse heart myoglobin.Scientific reports · 2023Article
18 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
2 authors at 1 institution in 1 country.
Funding
Abstract
Reverse turns are a major class of protein secondary structure; they represent sites of chain reversal and thus sites where the globular character of a protein is created. It has been speculated for many years that turns may nucleate the formation of structure in protein folding, as their propensity to occur will favor the approximation of their flanking regions and their general tendency to be hydrophilic will favor their disposition at the solvent-accessible surface. Reverse turns are local features, and it is therefore not surprising that their structural properties have been extensively studied using peptide models. In this article, we review research on peptide models of turns to test the hypothesis that the propensities of turns to form in short peptides will relate to the roles of corresponding sequences in protein folding. Turns with significant stability as isolated entities should actively promote the folding of a protein, and by contrast, turn sequences that merely allow the chain to adopt conformations required for chain reversal are predicted to be passive in the folding mechanism. We discuss results of protein engineering studies of the roles of turn residues in folding mechanisms. Factors that correlate with the importance of turns in folding indeed include their intrinsic stability, as well as their topological context and their participation in hydrophobic networks within the protein's structure.
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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.