(Q44298011)

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The coordination of the isomerization of a conserved non-prolyl cis peptide bond with the rate-limiting steps in the folding of dihydrofolate reductase

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Europe PubMed Central

1 December 2017

The coordination of the isomerization of a conserved non-prolyl cis peptide bond with the rate-limiting steps in the folding of dihydrofolate reductase (English)

1 reference

Europe PubMed Central

1 December 2017

author name string

Anna-Karin E Svensson

1

1 reference

Europe PubMed Central

1 December 2017

John C O'Neill

2

1 reference

Europe PubMed Central

1 December 2017

C Robert Matthews

3

1 reference

Europe PubMed Central

1 December 2017

language of work or name

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publication date

1 February 2003

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Europe PubMed Central

1 December 2017

Journal of Molecular Biology

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Europe PubMed Central

1 December 2017

326

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Europe PubMed Central

1 December 2017

2

1 reference

Europe PubMed Central

1 December 2017

569-583

1 reference

Europe PubMed Central

1 December 2017

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The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy

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Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy

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Folding of dihydrofolate reductase from Escherichia coli.

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Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

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Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions

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A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein

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Non-proline cis peptide bonds in proteins.

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An abinitio quantum-mechanical investigation on the rotational isomerism in amides and esters

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Multiple roles of prolyl residues in structure and folding

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Direct measurement indicates a slow cis/trans isomerization at the secondary amide peptide bond of glycylglycine

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Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli

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Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy.

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A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model.

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Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics

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Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

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Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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On-pathway versus off-pathway folding intermediates

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Effect of point mutations on the folding of globular proteins

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Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase.

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Highly divergent dihydrofolate reductases conserve complex folding mechanisms

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Long-range interactions within a nonnative protein

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10.1016/S0022-2836(02)01444-4

1 reference

Europe PubMed Central

1 December 2017

1 reference

Europe PubMed Central

1 December 2017

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