(Q35021976)

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Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Ana Rosa Viguera

1

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

author name string

Luis Serrano

2

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

language of work or name

0 references

publication date

28 April 2003

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

number of pages

6

1 reference

based on heuristic

inferred from page(s)

Proceedings of the National Academy of Sciences of the United States of America

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

100

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

10

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

5730-5735

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding

1 reference

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Cytochrome c folding pathway: kinetic native-state hydrogen exchange

1 reference

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Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads

1 reference

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Bergerac-SH3: "frustation" induced by stabilizing the folding nucleus.

1 reference

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Apparent two-state tendamistat folding is a sequential process along a defined route

1 reference

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8 July 2018

A kinetic folding intermediate probed by native state hydrogen exchange

1 reference

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A kinetically significant intermediate in the folding of barnase

1 reference

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Absence of stable intermediates on the folding pathway of barnase

1 reference

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Fast kinetics and mechanisms in protein folding

1 reference

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Protein folding intermediates and pathways studied by hydrogen exchange

1 reference

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Hydrogen exchange demonstrates three domains in aldolase unfold sequentially

1 reference

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The energetics of T4 lysozyme reveal a hierarchy of conformations

1 reference

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The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.

1 reference

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The native state conformational ensemble of the SH3 domain from alpha-spectrin

1 reference

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

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Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure

1 reference

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Contact order, transition state placement and the refolding rates of single domain proteins.

1 reference

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Hydrogen exchange studies of protein structure

1 reference

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An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core

1 reference

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Hydrogen exchange at equilibrium: a short cut for analysing protein-folding pathways?

1 reference

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Touring the landscapes: partially folded proteins examined by hydrogen exchange

1 reference

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Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature.

1 reference

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Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH.

1 reference

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1 reference

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Conformational analysis of peptides corresponding to beta-hairpins and a beta-sheet that represent the entire sequence of the alpha-spectrin SH3 domain.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=156269

8 July 2018

Protein folding intermediates: native-state hydrogen exchange

1 reference

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Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition.

1 reference

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Hydrogen exchange and structural dynamics of proteins and nucleic acids

2 references

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1 reference

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1 reference

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Lack of definable nucleation sites in the rate-limiting transition state of barnase under native conditions

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Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.

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Experimental study of the protein folding landscape: unfolding reactions in cytochrome c.

1 reference

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The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding

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Protein conformational stabilities can be determined from hydrogen exchange rates

1 reference

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Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange

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Amide protection in an early folding intermediate of cytochrome c

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Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation

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https://api.crossref.org/works/10.1073%2FPNAS.0837456100

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Identifiers

10.1073/PNAS.0837456100

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

2003PNAS..100.5730V

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

ResearchGate publication ID

0 references

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