Evidence map›Paper›PMID 30634485›Full record

ArticleLife (Basel, Switzerland)2019

Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals.

Michael S Wang, Kenric J Hoegler, Michael H Hecht

Open access · goldAbstract read
In one paragraph

Article in Life (Basel, Switzerland), 2019. 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
0.6field-weighted citation impact, top 34% of its field
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, 15 citations in OpenAlex.

  1. ACS central science · 2025
    Article
  2. Review
  3. Review
  4. Peptides En Route from Prebiotic to Biotic Catalysis.Accounts of chemical research · 2024
    Article
  5. 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

3 authors at 1 institution in 1 country.

Michael S WangDepartment of Chemistry, Princeton University, Princeton, NJ 08540, USA. msw5@princeton.edu.
Kenric J HoeglerDepartment of Molecular Biology, Princeton University, Princeton, NJ 08540, USA. kenhoegl@gmail.com.
Michael H HechtDepartment of Chemistry, Princeton University, Princeton, NJ 08540, USA. hecht@princeton.edu.ORCID 0000-0002-5538-9813
Princeton University · US

Funding

National Science Foundation MCB-1409402.
6 · The paper itself

Abstract

Life as we know it would not exist without the ability of protein sequences to bind metal ions. Transition metals, in particular, play essential roles in a wide range of structural and catalytic functions. The ubiquitous occurrence of metalloproteins in all organisms leads one to ask whether metal binding is an evolved trait that occurred only rarely in ancestral sequences, or alternatively, whether it is an innate property of amino acid sequences, occurring frequently in unevolved sequence space. To address this question, we studied 52 proteins from a combinatorial library of novel sequences designed to fold into 4-helix bundles. Although these sequences were neither designed nor evolved to bind metals, the majority of them have innate tendencies to bind the transition metals copper, cobalt, and zinc with high nanomolar to low-micromolar affinity.

Indexed as

binary patterned amino acid sequencesnovel metalloproteinsprebiotic chemistryprotein design

Identifiers

PMID30634485
PMCPMC6463171
OpenAlexW2909248178

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.