Hydrogen-deuterium exchange as a probe of folding and assembly in viral capsids

Journal of Molecular Biology

Volumn 306, Issue 3, 2001, Pages 389-396

  Tuma, Roman ^a   Coward, Lori U ^b   Kirk, Marion C ^b   Barnes, Stephen ^b,c   Prevelige Jr, Peter E ^a  

^a University of Alabama at Birmingham   (United States)

^b UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^c University of Alabama at Birmingham   (United States)

Author keywords

Capsid; Dynamics; Hydrogen deuterium exchange; Protein folding; Virus

Indexed keywords

CAPSID PROTEIN; DEUTERIUM; HYDROGEN; PEPSIN A; PROTEIN SUBUNIT;

ARTICLE; BACTERIOPHAGE; DNA PACKAGING; MACROMOLECULE; MASS SPECTROMETRY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN METABOLISM; PROTEIN STABILITY; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; VIRUS CAPSID;

MIRIDAE;

EID: 0035936693     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4383     Document Type: Article

References (28)

1. The cell as a collection of protein machines: Preparing the next generation of molecular biologists
2. Hydrogen exchange studies of respiratory proteins. 3. Structural and free energy changes in hemoglobin by use of a difference method
3. Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin
4. Conformational transformations in the protein lattice of phage P22 procapsids
5. Assembly of bacteriophage P22: A model for ds-DNA virus assembly
6. Mechanism of capsid maturation in a double-stranded DNA virus
7. Visualization of the maturation transition in bacteriophage P22 by electron cryomicroscopy
8. Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus
9. Subunit conformational changes accompanying bacteriophage P22 capsid maturation
10. Domain structure of the P22 coat protein
11. Mechanisms and uses of hydrogen exchange
12. Detection of transient protein folding populations by mass spectrometry
13. Investigation of protein folding by mass spectrometry
14. Conformation of cytochrome c studied by deuterium exchange-electrospray ionization mass spectrometry
15. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
16. Identification of unfolding domains in large proteins by their unfolding rates
17. Hydrogen exchange demonstrates three domains in aldolase unfold sequentially
18. Comparison of continuous and pulsed labeling amide hydrogen exchange/mass spectrometry for studies of protein dynamics
19. Identification of protein-protein interfaces by decreased amide proton solvent accessibility
20. Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
21. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
22. Characterization of subunit structural changes accompanying assembly of the bacteriophage P22 procapsid
23. The bacteriophage T4 DNA packaging apparatus targets the unexpanded prohead
24. Protein folding intermediates: Native-state hydrogen exchange
25. Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry
26. The use of structural information in the design of picornavirus capsid binding agents
27. Structure, interactions and dynamics of PRD1 virus. I. Coupling of subunit folding and capsid assembly
28. Mechanisms of virus assembly probed by Raman spectroscopy: The icosahedral bacteriophage P22