Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering (Q74518042)

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11 November 2019

title

Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering (English)

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X-ray scattering techniques

11 November 2019

main subject

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1

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11 November 2019

Tomonao Inobe

3

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11 November 2019

Yoshiyuki Amemiya

8

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11 November 2019

author name string

Kazuki Ito

2

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11 November 2019

Masaharu Nakao

4

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11 November 2019

Kosuke Maki

5

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11 November 2019

Kiyoto Kamagata

6

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11 November 2019

Hiroshi Kihara

7

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11 November 2019

Kunihiro Kuwajima

9

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11 November 2019

publication date

1 August 2002

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Journal of Molecular Biology

11 November 2019

published in

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11 November 2019

volume

321

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issue

1

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page(s)

121-132

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Intermediates in the folding reactions of small proteins

11 November 2019

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Stopped-Flow Apparatus for X-ray Scattering and XAFS

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Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering

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A lysozyme folding intermediate revealed by solution X-ray scattering.

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Chain collapse can occur concomitantly with the rate-limiting step in protein folding

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Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin

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Molten globule of cytochrome c studied by small angle X-ray scattering.

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Transition state in the folding of alpha-lactalbumin probed by the 6-120 disulfide bond

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Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin

7 January 2021

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Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering

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Time Resolved Collapse of a Folding Protein Observed with Small Angle X-Ray Scattering

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The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions.

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7 January 2021

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7 January 2021

Identifiers

DOI

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11 November 2019

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