Combining ultracentrifugation with fluorescence to follow the unfolding of modules 16-17 of complement receptor type 1

M D  Kirkitadze; K  Jumel; S E  Harding; D T F  Dryden; M  Krych; J P  Atkinson; P N  Barlow

Combining ultracentrifugation with fluorescence to follow the unfolding of modules 16-17 of complement receptor type 1

M D Kirkitadze, K Jumel, S E Harding, D T F Dryden, M Krych, J P Atkinson, P N Barlow

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Abstract / Description of output

Complement receptor type 1 (CR1) is a member of a family of regulators of complement activation with therapeutic potential. A fragment of CR1 comprising modules 16 and 17 was overexpressed as a recombinant nonglycosylated protein in Pichia pastoris. Intrinsic fluorescence studies of the unfolding of recombinant CR1 similar to 16-17 caused by increasing concentrations of guanidinium chloride revealed that the intermodular junction unfolds first, followed by module 17, with module 16 the last to unfold. Sedimentation velocity studies in the analytical ultracentrifuge revealed a corresponding clear change in conformation from the native macromolecules with an axial ratio of about 5:1 to a much more extended conformation.

Original language	English
Title of host publication	ANALYTICAL ULTRACENTRIFUGATION V
Editors	H Colfen
Place of Publication	BERLIN
Publisher	Springer
Pages	164-167
Number of pages	4
ISBN (Print)	3-540-66175-1
Publication status	Published - 1999
Event	11th Symposium on Analytical Ultracentrifugation - POTSDAM Duration: 25 Mar 1999 → 26 Mar 1999

Conference

Conference	11th Symposium on Analytical Ultracentrifugation
City	POTSDAM
Period	25/03/99 → 26/03/99

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@inproceedings{ff4ed0f4af3a4c30841794f2a040b0a5,

title = "Combining ultracentrifugation with fluorescence to follow the unfolding of modules 16-17 of complement receptor type 1",

abstract = "Complement receptor type 1 (CR1) is a member of a family of regulators of complement activation with therapeutic potential. A fragment of CR1 comprising modules 16 and 17 was overexpressed as a recombinant nonglycosylated protein in Pichia pastoris. Intrinsic fluorescence studies of the unfolding of recombinant CR1 similar to 16-17 caused by increasing concentrations of guanidinium chloride revealed that the intermodular junction unfolds first, followed by module 17, with module 16 the last to unfold. Sedimentation velocity studies in the analytical ultracentrifuge revealed a corresponding clear change in conformation from the native macromolecules with an axial ratio of about 5:1 to a much more extended conformation.",

author = "Kirkitadze, {M D} and K Jumel and Harding, {S E} and Dryden, {D T F} and M Krych and Atkinson, {J P} and Barlow, {P N}",

year = "1999",

language = "English",

isbn = "3-540-66175-1",

pages = "164--167",

editor = "H Colfen",

booktitle = "ANALYTICAL ULTRACENTRIFUGATION V",

publisher = "Springer",

address = "United Kingdom",

note = "11th Symposium on Analytical Ultracentrifugation ; Conference date: 25-03-1999 Through 26-03-1999",

}

TY - GEN

T1 - Combining ultracentrifugation with fluorescence to follow the unfolding of modules 16-17 of complement receptor type 1

AU - Kirkitadze, M D

AU - Jumel, K

AU - Harding, S E

AU - Dryden, D T F

AU - Krych, M

AU - Atkinson, J P

AU - Barlow, P N

PY - 1999

Y1 - 1999

N2 - Complement receptor type 1 (CR1) is a member of a family of regulators of complement activation with therapeutic potential. A fragment of CR1 comprising modules 16 and 17 was overexpressed as a recombinant nonglycosylated protein in Pichia pastoris. Intrinsic fluorescence studies of the unfolding of recombinant CR1 similar to 16-17 caused by increasing concentrations of guanidinium chloride revealed that the intermodular junction unfolds first, followed by module 17, with module 16 the last to unfold. Sedimentation velocity studies in the analytical ultracentrifuge revealed a corresponding clear change in conformation from the native macromolecules with an axial ratio of about 5:1 to a much more extended conformation.

AB - Complement receptor type 1 (CR1) is a member of a family of regulators of complement activation with therapeutic potential. A fragment of CR1 comprising modules 16 and 17 was overexpressed as a recombinant nonglycosylated protein in Pichia pastoris. Intrinsic fluorescence studies of the unfolding of recombinant CR1 similar to 16-17 caused by increasing concentrations of guanidinium chloride revealed that the intermodular junction unfolds first, followed by module 17, with module 16 the last to unfold. Sedimentation velocity studies in the analytical ultracentrifuge revealed a corresponding clear change in conformation from the native macromolecules with an axial ratio of about 5:1 to a much more extended conformation.

M3 - Conference contribution

SN - 3-540-66175-1

SP - 164

EP - 167

BT - ANALYTICAL ULTRACENTRIFUGATION V

A2 - Colfen, H

PB - Springer

CY - BERLIN

T2 - 11th Symposium on Analytical Ultracentrifugation

Y2 - 25 March 1999 through 26 March 1999

ER -

Combining ultracentrifugation with fluorescence to follow the unfolding of modules 16-17 of complement receptor type 1

Abstract / Description of output

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