Theoretical Studies of the Energetics and Dynamics of the Aqueous and Ionic Environment about Proteins: Crystals of Streptomyces Griseus Protease A

Proceedings of the First Donegani Scientific Workshop on Strategies for Computer Chemistry ◽

10.1007/978-94-009-2599-1_5 ◽

1989 ◽

pp. 31-32

Author(s):

F. Avbelj ◽

J. Moult ◽

D. H. Kitson ◽

M. N. G. James ◽

A. T. Hagler

Keyword(s):

Streptomyces Griseus ◽

Theoretical Studies ◽

Ionic Environment

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Molecular dynamics study of the structure and dynamics of a protein molecule in a crystalline ionic environment, Streptomyces griseus protease A

Biochemistry ◽

10.1021/bi00489a023 ◽

1990 ◽

Vol 29 (37) ◽

pp. 8658-8676 ◽

Cited By ~ 48

Author(s):

F. Avbelj ◽

J. Moult ◽

D. H. Kitson ◽

M. N. G. James ◽

A. T. Hagler

Keyword(s):

Molecular Dynamics ◽

Streptomyces Griseus ◽

Protein Molecule ◽

Structure And Dynamics ◽

Ionic Environment

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Conformational characterization of nucleosome structure by Electron Microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100146813 ◽

1993 ◽

Vol 51 ◽

pp. 194-195

Author(s):

Gregory J. Czarnota

Keyword(s):

Electron Microscopy ◽

Structural Changes ◽

Physiological State ◽

Gene Activation ◽

Three Dimensional ◽

Macromolecular Complex ◽

Ultrastructural Studies ◽

Ionic Environment ◽

Nucleosome Structure ◽

Dimensional Reconstruction

Chromatin structure at the fundamental level of the nucleosome is important in vital cellular processes. Recent biochemical and genetic analyses show that nucleosome structure and structural changes are very active participants in gene expression, facilitating or inhibiting transcription and reflecting the physiological state of the cell. Structural states and transitions for this macromolecular complex, composed of DNA wound about a heterotypic octamer of variously modified histone proteins, have been measured by physico-chemical techniques and by enzyme-accessibility and are recognized to occur with various post-translational modifications, gene activation, transformation and with ionic-environment. In spite of studies which indicate various forms of nucleosome structure, all current x-ray and neutron diffraction studies have consistently resulted in only one structure, suggestive of a static conformation. In contrast, two-dimensional electron microscopy studies and three-dimensional reconstruction techniques have yielded different structures. These fundamental differences between EM and other ultrastructural studies have created a long standing quandary, which I have addressed and resolved using spectroscopic electron microscopy and statistical analyses of nucleosome images in a study of nucleosome structure with ionic environment.

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