Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains (Q35130325)

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scholarly article

Language	Label	Description	Also known as
English	Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains	scholarly article

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

protein folding

0 references

author name string

Sarah Batey

1

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Jane Clarke

2

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

language of work or name

0 references

publication date

15 November 2006

1 reference

Europe PubMed Central

PubMed publication ID

6 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

6 August 2017

103

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

48

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

18113-18118

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Complex folding kinetics of a multidomain protein

1 reference

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Folding of spectrin's SH3 domain in the presence of spectrin repeats

1 reference

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Spectrin R16: broad energy barrier or sequential transition states?

1 reference

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13 July 2018

Cooperative folding in a multi-domain protein

1 reference

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Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase.

1 reference

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Biophysical investigations of engineered polyproteins: implications for force data

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Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity.

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Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer

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

1 reference

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Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation.

1 reference

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Stability and folding rates of domains spanning the large A-band super-repeat of titin

1 reference

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The scFv fragment of the antibody hu4D5-8: evidence for early premature domain interaction in refolding

1 reference

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Advances in structural genomics

1 reference

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Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil

1 reference

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13 July 2018

Recombination of protein domains facilitated by co-translational folding in eukaryotes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1636339

13 July 2018

The spectrin repeat folds into a three-helix bundle in solution.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1636339

13 July 2018

The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains

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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Crystal structure of the repetitive segments of spectrin

1 reference

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Erythrocyte spectrin is comprised of many homologous triple helical segments

1 reference

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Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens

1 reference

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Phasing the conformational unit of spectrin

1 reference

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13 July 2018

How do small single-domain proteins fold?

1 reference

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21 January 2018

Modular structure of the trigger factor required for high activity in protein folding

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0604580103

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Exploring the folding pathways of annexin I, a multidomain protein. I. non-native structures stabilize the partially folded state of the isolated domain 2 of annexin I.

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0604580103

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Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability

1 reference

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Titin; a multidomain protein that behaves as the sum of its parts

1 reference

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Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding

1 reference

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The folding mechanism of a two-domain protein: folding kinetics and domain docking of the gene-3 protein of phage fd.

1 reference

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Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0604580103

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Effects of domain dissection on the folding and stability of the 43 kDa protein PGK probed by NMR.

1 reference

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The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0604580103

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Folding mechanism of a multiple independently-folding domain protein: double B domain of protein A.

1 reference

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Independent Movement, Dimerization and Stability of Tandem Repeats of Chicken Brain α-Spectrin

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Co-operativity between modules within a C3b-binding site of complement receptor type 1

1 reference

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Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule?

1 reference

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Independently melting modules and highly structured intermodular junctions within complement receptor type 1

1 reference

https://pubmed.ncbi.nlm.nih.gov/17108086

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inferred from PubMed ID database lookup

Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity

1 reference

https://pubmed.ncbi.nlm.nih.gov/17108086

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Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons

1 reference

https://pubmed.ncbi.nlm.nih.gov/17108086

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Immunoglobulin-type domains of titin are stabilized by amino-terminal extension

1 reference

https://pubmed.ncbi.nlm.nih.gov/17108086

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based on heuristic

inferred from PubMed ID database lookup

Kinetic stabilisation of a modular protein by domain interactions

1 reference

https://pubmed.ncbi.nlm.nih.gov/17108086

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.0604580103

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

2006PNAS..10318113B

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ResearchGate publication ID

0 references

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