Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer

Ekkehard Kauffmann; Nicholas C. Darnton; Robert H. Austin; Carl Batt; Klaus Gerwert

doi:10.1073/pnas.101122898

Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer

Ekkehard Kauffmann
, Nicholas C. Darnton
, Robert H. Austin
, Carl Batt
, Klaus Gerwert

Research output: Contribution to journal › Article › peer-review

122 Scopus citations

Abstract

The extremely slow α-helix/β-sheet transition of proteins is a crucial step in amylogenic diseases and represents an internal rearrangement of local contacts in an already folded protein. These internal structural rearrangements within an already folded protein are a critical aspect of biological action and are a product of conformational flow along unknown metastable local minima of the energy landscape of the compact protein. We use a diffusional IR mixer with time-resolved Fourier transform IR spectroscopy capable of 400-μs time resolution to show that the trifluoroethanol driven β-sheet to α-helix transition of β-lactoglobulin proceeds via a compact β-sheet intermediate with a lifetime of 7 ms, small compared with the overall folding time of β-lactoglobulin.

Original language	English (US)
Pages (from-to)	6646-6649
Number of pages	4
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	98
Issue number	12
DOIs	https://doi.org/10.1073/pnas.101122898
State	Published - Jun 5 2001

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10.1073/pnas.101122898

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title = "Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer",

abstract = "The extremely slow α-helix/β-sheet transition of proteins is a crucial step in amylogenic diseases and represents an internal rearrangement of local contacts in an already folded protein. These internal structural rearrangements within an already folded protein are a critical aspect of biological action and are a product of conformational flow along unknown metastable local minima of the energy landscape of the compact protein. We use a diffusional IR mixer with time-resolved Fourier transform IR spectroscopy capable of 400-μs time resolution to show that the trifluoroethanol driven β-sheet to α-helix transition of β-lactoglobulin proceeds via a compact β-sheet intermediate with a lifetime of 7 ms, small compared with the overall folding time of β-lactoglobulin.",

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Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer. / Kauffmann, Ekkehard; Darnton, Nicholas C.; Austin, Robert H. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 98, No. 12, 05.06.2001, p. 6646-6649.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer

AU - Kauffmann, Ekkehard

AU - Darnton, Nicholas C.

AU - Austin, Robert H.

AU - Batt, Carl

AU - Gerwert, Klaus

PY - 2001/6/5

Y1 - 2001/6/5

N2 - The extremely slow α-helix/β-sheet transition of proteins is a crucial step in amylogenic diseases and represents an internal rearrangement of local contacts in an already folded protein. These internal structural rearrangements within an already folded protein are a critical aspect of biological action and are a product of conformational flow along unknown metastable local minima of the energy landscape of the compact protein. We use a diffusional IR mixer with time-resolved Fourier transform IR spectroscopy capable of 400-μs time resolution to show that the trifluoroethanol driven β-sheet to α-helix transition of β-lactoglobulin proceeds via a compact β-sheet intermediate with a lifetime of 7 ms, small compared with the overall folding time of β-lactoglobulin.

AB - The extremely slow α-helix/β-sheet transition of proteins is a crucial step in amylogenic diseases and represents an internal rearrangement of local contacts in an already folded protein. These internal structural rearrangements within an already folded protein are a critical aspect of biological action and are a product of conformational flow along unknown metastable local minima of the energy landscape of the compact protein. We use a diffusional IR mixer with time-resolved Fourier transform IR spectroscopy capable of 400-μs time resolution to show that the trifluoroethanol driven β-sheet to α-helix transition of β-lactoglobulin proceeds via a compact β-sheet intermediate with a lifetime of 7 ms, small compared with the overall folding time of β-lactoglobulin.

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DO - 10.1073/pnas.101122898

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AN - SCOPUS:0035811052

SN - 0027-8424

VL - 98

SP - 6646

EP - 6649

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

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

IS - 12

ER -

Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer

Abstract

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