ReviewJournal of structural and functional genomics2011
NMR-based structural biology of proteins in supercooled water.
Review in Journal of structural and functional genomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed.
- On the Use of Strong Proton Donors as a Tool for Overcoming Line Broadening in NMR: A Comment.Magnetic resonance in chemistry : MRC · 2025Article
- The 5'-terminal stem-loop RNA element of SARS-CoV-2 features highly dynamic structural elements that are sensitive to differences in cellular pH.Nucleic acids research · 2024Article
- From Protein Design to the Energy Landscape of a Cold Unfolding Protein.The journal of physical chemistry. B · 2022Article
- A Solution NMR Approach To Determine the Chemical Structures of Carbohydrates Using the Hydroxyl Groups as Starting Points.ACS omega · 2018Article
- MASBiophysical journal · 2016Article
- Using NMR and molecular dynamics to link structure and dynamics effects of the universal base 8-aza, 7-deaza, N8 linked adenosine analog.Nucleic acids research · 2016Article
- Crystal cryocooling distorts conformational heterogeneity in a model Michaelis complex of DHFR.Structure (London, England : 1993) · 2014Article
- Cold denaturation of a protein dimer monitored at atomic resolution.Nature chemical biology · 2013Article
- High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cold-induced changes in the protein ubiquitin.PloS one · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NMR-based structural biology of proteins can be pursued efficiently in supercooled water at temperatures well below the freezing point of water. This enables one to study protein structure, dynamics, hydration and cold denaturation in an unperturbed aqueous solution at very low temperatures. Furthermore, such studies enable one to accurately measure thermodynamic parameters associated with protein cold denaturation. Presently available approaches to acquire NMR data for supercooled aqueous protein solutions are surveyed, new insights obtained from such studies are summarized, and future perspectives are discussed.
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Registered trials
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.