scholarly journals STUDIES ON NUCLEAR STRUCTURE AND FUNCTION IN TETRAHYMENA PYRIFORMIS

1970 ◽  
Vol 47 (3) ◽  
pp. 619-630 ◽  
Author(s):  
Martin A. Gorovsky
Keyword(s):  
Electron Microscope ◽  
Outer Membrane ◽  
Nuclear Structure ◽  
Efficient Method ◽  
Tetrahymena Pyriformis ◽  
Structure And Function ◽  
Whole Cell ◽  
And Function

This report describes a rapid, efficient method for isolating macronuclei from Tetrahymena. The macronuclear fraction contains only small amounts of micronuclear material and little detectable whole cell or cytoplasmic contamination. A method is also described for preparing a "micronuclear fraction" which contains 20–40 micronuclei for every macronucleus present. Electron microscope observations indicate that the ultrastructure of the nuclei in the macronuclear fraction closely resembles that of nuclei in situ. The presence of ribosomes on the outer membrane of micronuclei and of pores in the micronuclear envelope is also described.

scholarly journals STUDIES ON NUCLEAR STRUCTURE AND FUNCTION IN TETRAHYMENA PYRIFORMIS

1970 ◽  
Vol 47 (3) ◽  
pp. 631-636 ◽  
Author(s):  
Martin A. Gorovsky
Keyword(s):  
Nuclear Structure ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Structure And Function ◽  
Polyacrylamide Gel ◽  
And Function

Histones were extracted from isolated macro- and micronuclear fractions and from nucleohistone fibers which were prepared from the isolated macronuclear fraction. Analysis of these histones by polyacrylamide gel electrophoresis indicated that there are electrophoretic differences between the histones of macro- and micronuclei.

Bacterial ß-Barrel Outer Membrane Proteins

2009 ◽  
pp. 182-207
Author(s):  
Pantelis G. Bagos ◽  
Stavros J. Hamodrakas
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Bacterial Cell ◽  
Outer Membrane Proteins ◽  
Structural Features ◽  
Structure And Function ◽  
Structural Motif ◽  
Functional Roles ◽  
Bacterial Outer Membrane ◽  
And Function

ß-barrel outer membrane proteins constitute the second and less well-studied class of transmembrane proteins. They are present exclusively in the outer membrane of Gram-negative bacteria and presumably in the outer membrane of mitochondria and chloroplasts. During the last few years, remarkable advances have been made towards an understanding of their functional and structural features. It is now wellknown that ß-barrels are performing a large variety of biologically important functions for the bacterial cell. Such functions include acting as specific or non-specific channels, receptors for various compounds, enzymes, translocation channels, structural proteins, and adhesion proteins. All these functional roles are of great importance for the survival of the bacterial cell under various environmental conditions or for the pathogenic properties expressed by these organisms. This chapter reviews the currently available literature regarding the structure and function of bacterial outer membrane proteins. We emphasize the functional diversity expressed by a common structural motif such as the ß-barrel, and we provide evidence from the current literature for dozens of newly discovered families of transmembrane ß-barrels.

scholarly journals Structure prediction of crystals, surfaces and nanoparticles

2020 ◽  
Vol 378 (2186) ◽  
pp. 20190600
Author(s):  
Scott M. Woodley ◽  
Graeme M. Day ◽  
R. Catlow
Keyword(s):  
Machine Learning ◽  
Energy Function ◽  
Structure Prediction ◽  
Search Algorithm ◽  
Structure And Function ◽  
Current Status ◽  
Organic Systems ◽  
And Function

We review the current techniques used in the prediction of crystal structures and their surfaces and of the structures of nanoparticles. The main classes of search algorithm and energy function are summarized, and we discuss the growing role of methods based on machine learning. We illustrate the current status of the field with examples taken from metallic, inorganic and organic systems. This article is part of a discussion meeting issue ‘Dynamic in situ microscopy relating structure and function’.

scholarly journals Primary structure and function of a cytotoxic outer-membrane protein (ComP) of Plesiomonas shigelloides

2008 ◽  
Vol 281 (1) ◽  
pp. 10-16 ◽  
Author(s):  
Hitoshi Tsugawa ◽  
Asako Ogawa ◽  
Satomi Takehara ◽  
Mayumi Kimura ◽  
Yoshio Okawa
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Primary Structure ◽  
Structure And Function ◽  
Plesiomonas Shigelloides ◽  
And Function
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