| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophysical Journal 66: 1631-1641 (1994)
© 1994 the Biophysical Society
Boston Biomedical Research Institute, Massachusetts 02114.
ABSTRACT
The pressure stability of bacteriophage P22 coat protein in both monomeric and polymeric forms under hydrostatic pressure was examined using light scattering, fluorescence emission, polarization, and lifetime methodology. The monomeric protein is very unstable toward pressure and undergoes significant structural changes at pressures as low as 0.5 kbar. These structural changes ultimately lead to denaturation of the subunit. Comparison of the protein denatured by pressure to that in guanidine hydrochloride suggests that pressure results in partial unfolding, perhaps by a domain mechanism. Fluorescence lifetime measurements indicate that at atmospheric pressure the local environments of the tryptophans are remarkably similar, suggesting they may be clustered. In contrast to the monomeric protein subunit, the protein when polymerized into procapsid shells is very stable to applied pressure and does not dissociate with pressure up to 2.5 kbar. However, under applied pressure the procapsid shells are cold-labile, suggesting they are entropically stabilized. The significance of these results in terms of virus assembly are discussed.
This article has been cited by other articles:
 |
|
 |
|
  L. M. T. R. Lima, D. Foguel, and J. L. Silva DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume PNAS, December 8, 2000; (2000) 250352197. [Abstract] [Full Text]
|
|
|
|
|
|
R. J. St. John, J. F. Carpenter, and T. W. Randolph High pressure fosters protein refolding from aggregates at high concentrations PNAS, November 9, 1999; 96(23): 13029 - 13033. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Mohana-Borges, J. Lima Silva, and G. de Prat-Gay Protein Folding in the Absence of Chemical Denaturants. REVERSIBLE PRESSURE DENATURATION OF THE NONCOVALENT COMPLEX FORMED BY THE ASSOCIATION OF TWO PROTEIN FRAGMENTS J. Biol. Chem., March 19, 1999; 274(12): 7732 - 7740. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Tuma, P. E. Prevelige Jr., and G. J. Thomas Jr. Mechanism of capsid maturation in a double-stranded DNA virus PNAS, August 18, 1998; 95(17): 9885 - 9890. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. L. Galisteo, C. L. Gordon, and J. King Stability of Wild-type and Temperature-sensitive Protein Subunits of the Phage P22 Capsid J. Biol. Chem., July 14, 1995; 270(28): 16595 - 16601. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Chapeaurouge, J. S. Johansson, and S. T. Ferreira Folding Intermediates of a Model Three-helix Bundle Protein. PRESSURE AND COLD DENATURATION STUDIES J. Biol. Chem., April 27, 2001; 276(18): 14861 - 14866. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. P. Gaspar, A. F. Terezan, A. S. Pinheiro, D. Foguel, M. A. Rebello, and J. L. Silva The Metastable State of Nucleocapsids of Enveloped Viruses as Probed by High Hydrostatic Pressure J. Biol. Chem., March 2, 2001; 276(10): 7415 - 7421. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. C. Oliveira, A. M. O. Gomes, F. C. L. Almeida, R. Mohana-Borges, A. P. Valente, V. S. Reddy, J. E. Johnson, and J. L. Silva Virus Maturation Targets the Protein Capsid to Concerted Disassembly and Unfolding J. Biol. Chem., May 19, 2000; 275(21): 16037 - 16043. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. M. T. R. Lima, D. Foguel, and J. L. Silva DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume PNAS, December 19, 2000; 97(26): 14289 - 14294. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
