Evidence map›Paper›PMID 22189917›Full record

ArticleProteins2012

Geofold: topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability.

Vibin Ramakrishnan, Sai Praveen Srinivasan, Saeed M Salem, Suzanne J Matthews, Wilfredo Colón, Mohammed Zaki, Christopher Bystroff

Abstract read
In one paragraph

Article in Proteins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Enhanced Thermostability of D-Psicose 3-Epimerase fromInternational journal of molecular sciences · 2021
    Article
  3. Article
  4. Article
  5. Exploring the folding pathway of green fluorescent protein through disulfide engineering.Protein science : a publication of the Protein Society · 2015
    Article
  6. 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

7 authors.

Vibin RamakrishnanCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
Sai Praveen Srinivasan
Saeed M Salem
Suzanne J Matthews
Wilfredo Colón
Mohammed Zaki
Christopher Bystroff

Funding

Computational design of specific binding proteins using Leave-One-OutR01GM099827 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI BONDOS, SARAH E, BYSTROFF, CHRISTOPHER · 2012 to 2021
$2.9M
Computational design of specific binding proteins using Leave-One-OutR21GM088838 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI BYSTROFF, CHRISTOPHER · 2009 to 2010
$397k
NIGMS NIH HHS R01 GM099827NIGMS NIH HHS R21 GM088838
6 · The paper itself

Abstract

Protein unfolding is modeled as an ensemble of pathways, where each step in each pathway is the addition of one topologically possible conformational degree of freedom. Starting with a known protein structure, GeoFold hierarchically partitions (cuts) the native structure into substructures using revolute joints and translations. The energy of each cut and its activation barrier are calculated using buried solvent accessible surface area, side chain entropy, hydrogen bonding, buried cavities, and backbone degrees of freedom. A directed acyclic graph is constructed from the cuts, representing a network of simultaneous equilibria. Finite difference simulations on this graph simulate native unfolding pathways. Experimentally observed changes in the unfolding rates for disulfide mutants of barnase, T4 lysozyme, dihydrofolate reductase, and factor for inversion stimulation were qualitatively reproduced in these simulations. Detailed unfolding pathways for each case explain the effects of changes in the chain topology on the folding energy landscape. GeoFold is a useful tool for the inference of the effects of disulfide engineering on the energy landscape of protein unfolding.

Indexed as

Protein UnfoldingSoftwareBacillusBacterial ProteinsBacteriophage T4DisulfidesEntropyEscherichia coliKineticsModels, MolecularMuramidaseMutationProtein ConformationProteinsProtein StabilityRibonucleasesBacillus amyloliquefaciens ribonucleaseBacterial ProteinsDisulfidesMuramidaseProteinsRibonucleasesTetrahydrofolate Dehydrogenase

Identifiers

PMID22189917
PMCPMC3277656

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.