Evidence map›Paper›PMID 29713036›Full record

ArticleNature chemistry2018

Engineering the entropy-driven free-energy landscape of a dynamic nanoporous protein assembly.

Robert Alberstein, Yuta Suzuki, Francesco Paesani, F Akif Tezcan

Abstract read
In one paragraph

Article in Nature chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

  1. Article
  2. Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Protein Assembly by Design.Chemical reviews · 2021
    Review
  7. Article
  8. Ion-dependent protein-surface interactions from intrinsic solvent response.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Role of Entropy in Colloidal Self-Assembly.Entropy (Basel, Switzerland) · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Robert AlbersteinDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.ORCID http://orcid.org/0000-0002-6655-8811
Yuta SuzukiDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
Francesco PaesaniDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA. fpaesani@ucsd.edu.
F Akif TezcanDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA. tezcan@ucsd.edu.ORCID http://orcid.org/0000-0002-4733-6500

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
NIGMS NIH HHS T32 GM008326
6 · The paper itself

Abstract

De novo design and construction of stimuli-responsive protein assemblies that predictably switch between discrete conformational states remains an essential but highly challenging goal in biomolecular design. We previously reported synthetic, two-dimensional protein lattices self-assembled via disulfide bonding interactions, which endows them with a unique capacity to undergo coherent conformational changes without losing crystalline order. Here, we carried out all-atom molecular dynamics simulations to map the free-energy landscape of these lattices, validated this landscape through extensive structural characterization by electron microscopy and established that it is predominantly governed by solvent reorganization entropy. Subsequent redesign of the protein surface with conditionally repulsive electrostatic interactions enabled us to predictably perturb the free-energy landscape and obtain a new protein lattice whose conformational dynamics can be chemically and mechanically toggled between three different states with varying porosities and molecular densities.

Indexed as

EntropyNanostructuresPorosityProtein EngineeringCrystallizationMicroscopy, ElectronMolecular Dynamics SimulationProteinsWaterProteinsWater

Identifiers

PMID29713036
PMCPMC6056010

What OpenQuestion holds

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Registered trials

None linked

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.