(Q36419990)

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Denaturation of RNA secondary and tertiary structure by urea: simple unfolded state models and free energy parameters account for measured m-values

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scholarly article

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Europe PubMed Central

PMC publication ID

14 August 2017

Denaturation of RNA secondary and tertiary structure by urea: simple unfolded state models and free energy parameters account for measured m-values (English)

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

1 reference

based on heuristic

inferred from title

author name string

Dominic Lambert

1

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

David E Draper

2

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

language of work or name

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publication date

29 October 2012

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

51

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

44

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

9014-9026

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer

1 reference

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Effects of Mg2+ on the free energy landscape for folding a purine riboswitch RNA.

1 reference

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1 reference

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The Osmolyte TMAO Stabilizes Native RNA Tertiary Structures in the Absence of Mg2+: Evidence for a Large Barrier to Folding from Phosphate Dehydration

1 reference

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Free State Conformational Sampling of the SAM-I Riboswitch Aptamer Domain

1 reference

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Dependence of RNA tertiary structural stability on Mg2+ concentration: interpretation of the Hill equation and coefficient

1 reference

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1 reference

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Urea destabilizes RNA by forming stacking interactions and multiple hydrogen bonds with nucleic acid bases

1 reference

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1 reference

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1 reference

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1 reference

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Global molecular structure and interfaces: refining an RNA:RNA complex structure using solution X-ray scattering data

1 reference

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Mutational Analysis of the Purine Riboswitch Aptamer Domain †

1 reference

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Metal-ion binding and metal-ion induced folding of the adenine-sensing riboswitch aptamer domain

1 reference

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Urea-amide preferential interactions in water: quantitative comparison of model compound data with biopolymer results using water accessible surface areas

1 reference

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30 September 2017

Folding of the adenine riboswitch

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3505219

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Predicting the energetics of osmolyte-induced protein folding/unfolding.

1 reference

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Structural basis for discriminative regulation of gene expression by adenine- and guanine-sensing mRNAs

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Crystal structure of a self-splicing group I intron with both exons

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TectoRNA: modular assembly units for the construction of RNA nano-objects

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Solution structure of a GAAA tetraloop receptor RNA

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1 reference

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

1 reference

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1 reference

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1 reference

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The nature of the accessible and buried surfaces in proteins

1 reference

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Effects of osmolytes on RNA secondary and tertiary structure stabilities and RNA-Mg2+ interactions

1 reference

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Use of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding

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1 reference

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1 reference

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1 reference

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inferred from PubMed ID database lookup

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1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

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inferred from PubMed ID database lookup

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1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

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1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

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based on heuristic

inferred from PubMed ID database lookup

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

12 December 2020

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inferred from PubMed ID database lookup

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1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

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based on heuristic

inferred from PubMed ID database lookup

The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes

1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Modeling unfolded states of peptides and proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

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based on heuristic

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Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility

1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

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1 reference

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/23088364

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI301103J

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

release_w6iq3kl3qbe4hn7dbt3rdlcg3i

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https://api.fatcat.wiki/v0/release/w6iq3kl3qbe4hn7dbt3rdlcg3i

24 November 2022

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PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

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