Structure and function of tetanus toxin. Approaches by DNA and protein chemistry

Toxicon ◽  
1989 ◽  
Vol 27 (1) ◽  
pp. 24-25
Keyword(s):  
Tetanus Toxin ◽  
Structure And Function ◽  
Protein Chemistry ◽  
And Function

Address of the President Sir Andrew Huxley, O.M. at the Anniversary Meeting, 30 November 1983

1984 ◽  
Vol 220 (1221) ◽  
pp. 383-398 ◽  
Keyword(s):  
Immune Complex ◽  
Complement System ◽  
Specific Antigen ◽  
Structure And Function ◽  
Protein Chemistry ◽  
Large Molecules ◽  
Protein Components ◽  
And Function ◽  
Polypeptide Chains ◽  
The Complement System

The Copley Medal is awarded to Professor R. R. Porter, F. R. S., in recognition of his elucidation of the structure of immunoglobulins and of the reactions involved in activating the complement system of proteins. Professor Porter and his colleagues, before 1970, were responsible for major contributions to the study of the structure of immunoglobulins. They showed that the molecule consists of two pairs of polypeptide chains with the specific antigen-combining sites associated with part of these chain structures. He received a Nobel prize for this work in 1972. He and his group have continued to make outstanding and fundamental contributions to the protein chemistry of immunology. They have determined the structure of C1q, the protein that binds to the immune complex and initiates the controlled cascade of proteolytic reactions leading to cell lysis. They have made major contributions to the structural elucidation of several other protein components of this reaction cascade and have identified domains of these large molecules that are catalytic centres or are involved in the formation of activated or inhibitory complexes. They are currently studying the structure and function of these complexes and their components. His work has been characterized by protein chemistry of the highest standard and his studies have been fundamental to our understanding of immunological processes, with wide repercussions on the understanding of disease and its prevention.

The Outer Membrane Took Center Stage

2018 ◽  
Vol 72 (1) ◽  
pp. 1-24
Author(s):  
Volkmar Braun
Keyword(s):  
Outer Membrane ◽  
Focal Point ◽  
Outer Membrane Proteins ◽  
Protein Composition ◽  
Structure And Function ◽  
General Interest ◽  
Protein Chemistry ◽  
Iron Chelates ◽  
And Function ◽  
Energy Dependent

My interest in membranes was piqued during a lecture series given by one of the founders of molecular biology, Max Delbrück, at Caltech, where I spent a postdoctoral year to learn more about protein chemistry. That general interest was further refined to my ultimate research focal point—the outer membrane of Escherichia coli—through the influence of the work of Wolfhard Weidel, who discovered the murein (peptidoglycan) layer and biochemically characterized the first phage receptors of this bacterium. The discovery of lipoprotein bound to murein was completely unexpected and demonstrated that the protein composition of the outer membrane and the structure and function of proteins could be unraveled at a time when nothing was known about outer membrane proteins. The research of my laboratory over the years covered energy-dependent import of proteinaceous toxins and iron chelates across the outer membrane, which does not contain an energy source, and gene regulation by iron, including transmembrane transcriptional regulation.

Chemiosmotic systems in medicine

1991 ◽  
Vol 11 (6) ◽  
pp. 445-475 ◽  
Author(s):  
Peter B. Garland
Keyword(s):  
Molecular Biology ◽  
Pharmacological Treatment ◽  
Structure And Function ◽  
The Other ◽  
Protein Chemistry ◽  
Structural Protein ◽  
Prokaryotic Cell ◽  
Functional Relationships ◽  
And Function ◽  
Different Levels

The concept of chemiosmotic systems arises from the pioneering work of Peter Mitchell on two fronts. One is concerned with the mechanisms by which molecules are transported across membranes which are generally barriers to such transport. These mechanisms are inevitably molecular, and are now yielding their secrets to a combination of structural protein chemistry and molecular biology. The other front is more physiological, and explores the functional relationships between metabolism and transport. Nevertheless, the two fronts form a continuum of mutally related structure and function. Chemiosmotic systems provide a hierarchy of complexity, starting from say a uniporter reconstituted in a chemically defined bilayer, and proceeding to greater complexity in mitochondria, chloroplasts, eukaryotic and prokaryotic cell membranes, and multicellular systems. Their relationship to medicine is profound, because they provide many opportunities for therapeutic intervention. In this paper I present an overview of chemiosmotic systems at different levels of complexity, both molecular and biological, of their involvements in pathology, and of possible pharmacological treatment or prevention of disease.

Use of antibodies in the study of protein structure and function in lung diseases

1991 ◽  
Vol 260 (2) ◽  
pp. L1-L12
Author(s):  
E. J. Miller ◽  
A. B. Cohen
Keyword(s):  
Lung Diseases ◽  
Current Knowledge ◽  
Function Analysis ◽  
Three Dimensional ◽  
Structure And Function ◽  
Protein Chemistry ◽  
Modern Biology ◽  
Protein Molecules ◽  
And Function ◽  
Structure Of Proteins

Proteins normally fold in a variety of three-dimensional structures. This variety of forms accounts for a multiplicity of functions. One of the major undertakings of modern biochemistry is to determine the structure of a given protein and in doing so learn about its function. Much of the effort in the field of protein chemistry is currently focused on defining areas or domains within the molecule that are responsible for its function. Antibodies specific for functional domains on a protein have been powerful tools in these studies and have provided a great deal of the current knowledge related to the location and function of well-defined structural areas within the protein molecules. The use of antibodies in the study of proteins has considerably advanced our knowledge of both the structure of proteins and their interaction with other molecules. In reviewing the use of antibodies for structure and/or function analysis, we have tried not only to review the techniques and applications involving antibodies but also to show how useful antibody reagents may be designed and prepared. In this review, some of the newer uses of antibodies in modern biology will be described, and a few illustrations of each will be provided.

Address of the President Sir Andrew Huxley, O. M. at the Anniversary Meeting, 30 November 1983

1984 ◽  
Vol 391 (1801) ◽  
pp. 215-230 ◽  
Keyword(s):  
Immune Complex ◽  
Complement System ◽  
Specific Antigen ◽  
Structure And Function ◽  
Protein Chemistry ◽  
Large Molecules ◽  
Protein Components ◽  
And Function ◽  
Polypeptide Chains ◽  
The Complement System

The Copley Medal is awarded to Professor R. R. Porter, F. R. S., in recognition of his elucidation of the structure of immunoglobulins and of the reactions involved in activating the complement system of proteins. Professor Porter and his colleagues, before 1970, were responsible for major contributions to the study of the structure of immunoglobulins. They showed that the molecule consists of two pairs of polypeptide chains with the specific antigen-combining sites associated with part of these chain structures. He received a Nobel prize for this work in 1972. He and his group have continued to make outstanding and fundamental contributions to the protein chemistry of immunology. They have determined the structure of C1q, the protein that binds to the immune complex and initiates the controlled cascade of proteolytic reactions leading to cell lysis. They have made major contributions to the structural elucidation of several other protein components of this reaction cascade and have identified domains of these large molecules that are catalytic centres or are involved in the formation of activated or inhibitory complexes. They are currently studying the structure and function of these complexes and their components. His work has been characterized by protein chemistry of the highest standard and his studies have been fundamental to our understanding of immunological processes, with wide repercussions on the understanding of disease and its prevention.

scholarly journals Monoclonal antibodies as probes of tetanus toxin structure and function.

1983 ◽  
Vol 42 (3) ◽  
pp. 942-948 ◽  
Author(s):  
J G Kenimer ◽  
W H Habig ◽  
M C Hardegree
Keyword(s):  
Monoclonal Antibodies ◽  
Tetanus Toxin ◽  
Structure And Function ◽  
And Function

Structure and function of neural networks in the retina

1988 ◽  
Vol 46 ◽  
pp. 26-27
Author(s):  
Peter Sterling
Keyword(s):  
Ganglion Cells ◽  
Three Dimensional ◽  
Structure And Function ◽  
Synaptic Connections ◽  
Visual Axis ◽  
One Dimensional ◽  
Cat Retina ◽  
Ultrathin Sections ◽  
And Function ◽  
Insight Into

The synaptic connections in cat retina that link photoreceptors to ganglion cells have been analyzed quantitatively. Our approach has been to prepare serial, ultrathin sections and photograph en montage at low magnification (˜2000X) in the electron microscope. Six series, 100-300 sections long, have been prepared over the last decade. They derive from different cats but always from the same region of retina, about one degree from the center of the visual axis. The material has been analyzed by reconstructing adjacent neurons in each array and then identifying systematically the synaptic connections between arrays. Most reconstructions were done manually by tracing the outlines of processes in successive sections onto acetate sheets aligned on a cartoonist's jig. The tracings were then digitized, stacked by computer, and printed with the hidden lines removed. The results have provided rather than the usual one-dimensional account of pathways, a three-dimensional account of circuits. From this has emerged insight into the functional architecture.

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