Stable folding core in the folding transition state of an alpha-helical integral membrane protein. (Q35180786)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21831834%20AND%20SRC:MED&resulttype=core&format=json

10 February 2020

title

Stable folding core in the folding transition state of an alpha-helical integral membrane protein (English)

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10 February 2020

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1

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10 February 2020

Paula Booth

series ordinal

6

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10 February 2020

2

Natalie D Di Bartolo

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10 February 2020

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Kathleen M Moreton

3

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10 February 2020

Oluseye O Ajoje

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4

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10 February 2020

Nicholas P Saggese

series ordinal

5

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10 February 2020

language of work or name

English

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publication date

9 August 2011

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

10 February 2020

published in

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10 February 2020

volume

108

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10 February 2020

issue

34

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10 February 2020

page(s)

14133-14138

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The transition state for folding of an outer membrane protein

10 February 2020

cites work

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Mapping the structure of an integral membrane protein under semi-denaturing conditions by laser-induced oxidative labeling and mass spectrometry.

13 July 2018

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13 July 2018

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The transition state for integral membrane protein folding

13 July 2018

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13 July 2018

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Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding

13 July 2018

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13 July 2018

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Is there or isn't there? The case for (and against) residual structure in chemically denatured proteins

13 July 2018

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The analysis of protein folding kinetic data produced in protein engineering experiments

13 July 2018

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Phi-value analysis and the nature of protein-folding transition states

13 July 2018

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Side-chain contributions to membrane protein structure and stability

13 July 2018

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Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state

13 July 2018

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13 July 2018

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Characterisation of the transition states for protein folding: towards a new level of mechanistic detail in protein engineering analysis

13 July 2018

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Unravelling the folding of bacteriorhodopsin

13 July 2018

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Ordered membrane insertion of an archaeal opsin in vivo.

13 July 2018

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Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism

13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain

13 July 2018

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13 July 2018

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13 July 2018

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Analysis of conformational changes in bacteriorhodopsin upon retinal removal

13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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13 July 2018

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21 January 2018

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Using micellar mole fractions to assess membrane protein stability in mixed micelles

21 January 2018

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Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR

21 January 2018

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Slow α Helix Formation during Folding of a Membrane Protein†

25 October 2018

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A biophysical study of integral membrane protein folding

21 January 2018

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12 December 2020

Secondary structure of bacteriorhodopsin fragments. External sequence constraints specify the conformation of transmembrane helices

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12 December 2020

Membrane insertion kinetics of a protein domain in vivo. The bacterioopsin n terminus inserts co-translationally

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12 December 2020

Experimental characterization of the denatured state ensemble of proteins

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12 December 2020

Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions

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12 December 2020

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12 December 2020

Identifiers

DOI

10.1073/PNAS.1012594108

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21831834%20AND%20SRC:MED&resulttype=core&format=json

10 February 2020

0 references

1 reference

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10 February 2020

PubMed publication ID

21831834

1 reference