Trimeric domain-swapped barnase (Q27766846)

scientific article

Language	Label	Description	Also known as
English	Trimeric domain-swapped barnase	scientific article

Statements

instance of

scholarly article

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title

Trimeric domain-swapped barnase (English)

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3

L Wyns

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author name string

I Zegers

series ordinal

1

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J Deswarte

series ordinal

2

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language of work or name

English

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publication date

2 February 1999

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published in

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

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volume

96

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issue

3

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page(s)

818-22

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cites work

Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography

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PubMed Central

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20 March 2017

The 2.0-A resolution crystal structure of a trimeric antibody fragment with noncognate VH-VL domain pairs shows a rearrangement of VH CDR3

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20 March 2017

Crystal structure of RNase T1 with 3'-guanylic acid and guanosine

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20 March 2017

Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution

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PubMed Central

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20 March 2017

The CCP4 suite: programs for protein crystallography

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20 March 2017

Principles of protein-protein interactions

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20 March 2017

Improved methods for building protein models in electron density maps and the location of errors in these models

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PubMed Central

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20 March 2017

Nucleation mechanisms in protein folding

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PubMed Central

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20 March 2017

A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding

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PubMed Central

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20 March 2017

The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure

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PubMed Central

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20 March 2017

The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability

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PubMed Central

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20 March 2017

Initiation sites of protein folding by NMR analysis

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29 September 2017

The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase

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29 September 2017

Molecular structure of a new family of ribonucleases

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29 September 2017

Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly

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2 June 2018

AMoRe: an automated package for molecular replacement

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Crossref

reference URL

https://api.crossref.org/works/10.1073%2FPNAS.96.3.818

retrieved

21 January 2018

Folding intermediates of wild-type and mutants of barnase. I. Use of phi-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium

1 reference

stated in

Crossref

reference URL

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retrieved

21 January 2018

Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity

1 reference

stated in

Crossref

reference URL

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retrieved

21 January 2018

Surface, subunit interfaces and interior of oligomeric proteins

1 reference

stated in

Crossref

reference URL

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retrieved

21 January 2018

The A-State of Barnase

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1073%2FPNAS.96.3.818

retrieved

21 January 2018

Identifiers

DOI

10.1073/PNAS.96.3.818

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PubMed publication ID

9927651

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ResearchGate publication ID

13360880

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Trimeric domain-swapped barnase (Q27766846)

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Trimeric domain-swapped barnase (Q27766846)

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