Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Alternative computational protocols for supercharging protein surfaces for reversible unfolding and retention of stability.

PloS one - 1 Jan 2013

Der Bryan S, Kluwe Christien, Miklos Aleksandr E, Jacak Ron, Lyskov Sergey, Gray Jeffrey J, Georgiou George, Ellington Andrew D, Kuhlman Brian

Abstract excerpt

Reengineering protein surfaces to exhibit high net charge, referred to as "supercharging", can improve reversibility of unfolding by preventing aggregation of partially unfolded states. Incorporation of charged side chains should be optimized while considering structural and energetic consequences, as numerous mutations and accumulation of like-charges can also destabilize the native state. A previously...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Green Fluorescent Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Protein Engineering

Share to Protein Stability

Share to Protein Unfolding

Share to Static Electricity

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 23741319
DOI: 10.1371/journal.pone.0064363
PMCID: PMC3669367

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Alternative computational protocols for supercharging protein surfaces for reversible unfolding and retention of stability.PMID 23741319Read ↗

Anion solvation enhanced by positive supercharging mutations preserves thermal stability of an antibody in a wide pH range.Semantic proximity Read ↗

Rational modification of protein stability by targeting surface sites leads to complicated results.Semantic proximity Read ↗

Conferring thermostability to mesophilic proteins through optimized electrostatic surfaces.Semantic proximity Read ↗

Alchemical Calculation of Relative Free Energies for Charge-Changing Mutations at Protein-Protein Interfaces Considering Fixed and Variable Protonation States.Semantic proximity Read ↗

The effect of charge mutations on the stability and aggregation of a human single chain Fv fragment.Semantic proximity Read ↗

Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations.Semantic proximity Read ↗

Residue-Specific Dock-Loosen-Unfold Mechanism of GB1 on Nanoparticle Surfaces Revealed by Kinetic and Φ-Value Analysis.Semantic proximity Read ↗

Charge Interactions in a Highly Charge-Depleted Protein.Semantic proximity Read ↗

Free-energy landscapes of membrane co-translocational protein unfolding.Semantic proximity Read ↗

To charge or not to charge?Semantic proximity Read ↗

Modulation of buried ionizable groups in proteins with engineered surface charge.Semantic proximity Read ↗

Implementing and Assessing an Alchemical Method for Calculating Protein-Protein Binding Free Energy.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.