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Global fluctuations of the immunoglobulin domains under physiological conditions

✍ Scribed by Yasushi Kawata; Kozo Hamaguchi

Publisher: Wiley (John Wiley & Sons)
Year: 1990
Tongue: English
Weight: 473 KB
Volume: 30
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360300316

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✦ Synopsis

Hydrogen-exchange rates of the indole NH proton of a tryptophan residue, buried fully in the interior of each of the constant (C,) and variable ( V , ) fragments of a type-x-immunoglobulin light chain, were studied at various pH values and at 25°C under 'H-nuclear magnetic resonance. The activation energies for the exchange reactions were determined also and compared with those for the unfolding reactions of these fragments induced by guanidine hydrochloride. The pH profiles of the exchange rates of the C L ( ~) and V L ( ~) fragments were very similar to that for a CL ( A ) fragment reported p r e v i ~u s l y . ~ It was found that the CL( K ) and VL( K ) fragments as well as the C,(A) fragment undergo a global unfolding transition with a conformation very similar to that of the fully unfolded state induced by guanidine hydrochloride even under physiological conditions.

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