Evidence map›Paper›PMID 34845603›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Site-Specific Interrogation of Protein Structure and Stability.

Debopreeti Mukherjee, Ismail A Ahmed, Feng Gai

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
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.

Debopreeti Mukherjee *Department of Chemistry, University of Pennsylvania, Philadelphia, PA, USA.
Ismail A Ahmed *Department of Biochemistry and Molecular Biophysics, University of Pennsylvania, Philadelphia, PA, USA.
Feng GaiDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, USA. gai@sas.upenn.edu.
University of Pennsylvania · US

Funding

Multidisciplinary Training in Cardiovascular BiologyT32HL007954 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI DAVIES, PETER FRANCIS · 2000 to 2019
$9.9M
ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
NHLBI NIH HHS T32 HL007954NIGMS NIH HHS P41 GM104605
6 · The paper itself

Abstract

To execute their function or activity, proteins need to possess variability in local electrostatic environment, solvent accessibility, structure, and stability. However, assessing any protein property in a site-specific manner is not easy since native spectroscopic signals often lack the needed specificity. One strategy that overcomes this limitation is to use unnatural amino acids that exhibit distinct spectroscopic features. In this chapter, we describe several such unnatural amino acids (UAAs) and their respective applications in site-specific interrogation of protein structure and stability using standard biophysical methods, including circular dichroism (CD), infrared (IR), and fluorescence spectroscopies.

Indexed as

Protein ConformationAmino AcidsCircular DichroismProteinsSpectrum AnalysisAmino AcidsProteinsCircular dichroism spectroscopyFluorescence spectroscopyInfrared spectroscopyProtein stabilityProtein structureSite-specific spectroscopic probeUnnatural amino acidUnnatural amino acid incorporation

Identifiers

PMID34845603
OpenAlexW3217182288

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.