An enzymatic molten globule: efficient coupling of folding and catalysis. (Q37511760)

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31 December 2019

title

An enzymatic molten globule: efficient coupling of folding and catalysis (English)

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31 December 2019

2

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31 December 2019

author name string

Katherina Vamvaca

1

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31 December 2019

Peter Kast

3

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31 December 2019

Konstantin Pervushin

4

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31 December 2019

Donald Hilvert

5

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31 December 2019

language of work or name

English

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publication date

20 August 2004

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

31 December 2019

published in

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31 December 2019

volume

101

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31 December 2019

issue

35

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31 December 2019

page(s)

12860-12864

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Solution structure of ade novoprotein from a designed combinatorial library

31 December 2019

cites work

1 reference

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Antibody multispecificity mediated by conformational diversity

23 August 2017

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Multiple conformational changes in enzyme catalysis

23 August 2017

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Intrinsic disorder and protein function

23 August 2017

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Coupling of folding and binding for unstructured proteins

23 August 2017

1 reference

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Investigating and Engineering Enzymes by Genetic Selection

23 August 2017

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Protein misfolding, evolution and disease

23 August 2017

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Redesigning enzyme topology by directed evolution

23 August 2017

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Hydrogen exchange: the modern legacy of Linderstrøm-Lang

23 August 2017

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Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry

23 August 2017

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Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=516485

Sequence space, folding and protein design

23 August 2017

1 reference

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Protein design: a hierarchic approach.

23 August 2017

1 reference

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‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=516485

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

23 August 2017

1 reference

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Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe

23 August 2017

1 reference

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Inactivation precedes overall molecular conformation changes during enzyme denaturation

23 August 2017

1 reference

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A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii

28 September 2017

1 reference

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Ligand binding energy and catalytic efficiency from improved packing within receptors and enzymes

26 June 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0404109101

Double point mutant F34W/W140F of staphylococcal nuclease is in a molten globule state but highly competent to fold into a functional conformation.

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0404109101

Defining the core structure of the α-lactalbumin molten globule state 1 1Edited by C. R. Matthews

21 January 2018

1 reference

12 December 2020

Alpha-Lactalbumin: compact state with fluctuating tertiary structure?

1 reference

12 December 2020

Catalytic molten globules

1 reference

12 December 2020

Conformational diversity and protein evolution--a 60-year-old hypothesis revisited

1 reference

12 December 2020

Evidence for a molten globule state as a general intermediate in protein folding

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.0404109101

1 reference

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31 December 2019

0 references

1 reference

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31 December 2019

PubMed publication ID

15322276

1 reference