Evidence map›Paper›PMID 27626127›Full record

ArticleThe journal of physical chemistry. B2016

The Missing Electrostatic Interactions Between DNA Substrate and Sulfolobus solfataricus DNA Photolyase: What is the Role of Charged Amino Acids in Thermophilic DNA Binding Proteins?

Yvonne M Gindt, Ban H Edani, Antonia Olejnikova, Ariana N Roberts, Sudipto Munshi, Robert J Stanley

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Characterization of a cold-adapted DNA photolyase from C. psychrerythraea 34H.Extremophiles : life under extreme conditions · 2017
    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

6 authors at 2 institutions in 1 country.

Yvonne M GindtDepartment of Chemistry and Biochemistry, Montclair State University , 1 Normal Avenue, Montclair, New Jersey 07043, United States.
Ban H EdaniDepartment of Chemistry and Biochemistry, Montclair State University , 1 Normal Avenue, Montclair, New Jersey 07043, United States.
Antonia OlejnikovaDepartment of Chemistry and Biochemistry, Montclair State University , 1 Normal Avenue, Montclair, New Jersey 07043, United States.
Ariana N RobertsDepartment of Chemistry and Biochemistry, Montclair State University , 1 Normal Avenue, Montclair, New Jersey 07043, United States.
Sudipto MunshiDepartment of Chemistry, Temple University , 1801 N Broad Street, Philadelphia, Pennsylvania 19122, United States.
Robert J StanleyDepartment of Chemistry, Temple University , 1801 N Broad Street, Philadelphia, Pennsylvania 19122, United States.
Montclair State University · USTemple University · US

Funding

Shared Services Center NASA 80NSSC17K0033
6 · The paper itself

Abstract

DNA photolyase can be used to study how a protein with its required cofactor has adapted over a large temperature range. The enzymatic activity and thermodynamics of substrate binding for protein from Sulfolobus solfataricus were directly compared to protein from Escherichia coli. Turnover numbers and catalytic activity were virtually identical, but organic cosolvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by ∼2 kJ/mol. The enthalpy of binding is ∼10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding was observed when ionic strength studies were used to separate binding interactions into electrostatic and nonelectrostatic contributions; DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein.

Indexed as

Static ElectricityTemperatureAmino AcidsCalorimetryDeoxyribodipyrimidine Photo-LyaseDNADNA-Binding ProteinsSulfolobus solfataricusAmino AcidsDeoxyribodipyrimidine Photo-LyaseDNADNA-Binding Proteins

Identifiers

PMID27626127
PMCPMC7301758
OpenAlexW2520278620

What OpenQuestion holds

Textmetadata
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.