NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding (Q30175424)

From Wikidata

Jump to navigation Jump to search

scientific article

edit

Language	Label	Description	Also known as
English	NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding	scientific article

Statements

instance of

scholarly article

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

title

NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding (English)

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

main subject

protein folding

0 references

OB-fold nucleic acid binding domain

1 reference

based on heuristic

inferred from title

author name string

Alexandrescu AT

series ordinal

1

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

Jaravine VA

series ordinal

2

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

Dames SA

series ordinal

3

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

Lamour FP

series ordinal

4

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

language of work or name

English

0 references

publication date

1 June 1999

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

published in

Journal of Molecular Biology

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

volume

289

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

issue

4

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

page(s)

1041-1054

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

cites work

Characterization of the free energy spectrum of peptostreptococcal protein L

1 reference

stated in

COCI

retrieved

9 October 2024

reference URL

https://opencitations.net/index/api/v1/citations/10.1016/S1359-0278(97)00038-2

Functional rapidly folding proteins from simplified amino acid sequences.

1 reference

stated in

COCI

retrieved

9 October 2024

reference URL

https://opencitations.net/index/api/v1/citations/10.1038/NSB1097-805

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

1 reference

stated in

COCI

retrieved

9 October 2024

reference URL

https://opencitations.net/index/api/v1/citations/10.1006/JMBI.1998.1645

Identifiers

DOI

10.1006/JMBI.1999.2813

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

PubMed publication ID

10369781

1 reference

stated in

Europe PubMed Central

PubMed publication ID

10369781

retrieved

9 June 2017

ResearchGate publication ID

12928845

0 references

 

Sitelinks

Wikipedia(0 entries)

edit

Wikibooks(0 entries)

edit

Wikinews(0 entries)

edit

Wikiquote(0 entries)

edit

Wikisource(0 entries)

edit

Wikiversity(0 entries)

edit

Wikivoyage(0 entries)

edit

Wiktionary(0 entries)

edit

Multilingual sites(0 entries)

edit

Retrieved from "https://www.wikidata.org/w/index.php?title=Q30175424&oldid=2258454794"