Edward Steers

Bio: Edward Steers is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Escherichia coli & Tetramer. The author has an hindex of 15, co-authored 25 publications receiving 1963 citations.

Principles that Govern the Folding of Protein Chains

Abstract: Stanford Moore, William Stein, and Anfinsen were awarded the Nobel Prize in Chemistry in 1972 for \"their contribution to the understanding of the connection between chemical structure and catalytic activity of the active center of the ribonuclease molecule.\" In his Nobel Lecture, Anfinsen provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the \"Thermodynamic Hypothesis,\" and outlined potential avenues of current and future scientific exploration.

[31] Affinity chromatography

Abstract: Publisher Summary The selective isolation and purification of enzymes and other biologically important macromolecules by “affinity chromatography” exploits the unique biological property of the proteins or polypeptides to bind ligands specifically and reversibly Affinity chromatography exploits the phenomenon of specific biological interaction in a large variety of protein–ligand systems A solution containing the macromolecule to be purified is passed through a column containing an insoluble polymer or gel to which a specific competitive inhibitor or other ligand has been covalently attached Proteins not exhibiting appreciable affinity for the ligand pass unretarded through the column, whereas those which recognize the inhibitor are retarded in proportion to the affinity existing under the experimental conditions The specifically adsorbed protein can be eluted by altering the composition of the solvent so that dissociation occurs Affinity chromatography may be useful in concentrating dilute solutions of proteins, in removing denatured forms of a purified protein, and in the separation and resolution of protein components resulting from specific chemical modifications of purified proteins Inherent advantages of this method of purification are the rapidity and ease of a potentially single-step procedure, the rapid separation of the protein to be purified from inhibitors and destructive contaminants, such as proteases, and protection from denaturation during purification by active site ligand-stabilization of protein tertiary structure

THE ORGANIZATION OF PROTEINS IN THE HUMAN RED BLOOD CELL MEMBRANE A Review

Abstract: The elucidation of the molecular architecture of cell membranes is a central goal for cell biology, as structure lies at the heart of function. The erythrocyte plasma membrane has long provided a favored testing ground for this inquiry. Human red blood cells are readily available, relatively homogeneous, and relevant to medicine. Their plasma membranes can be easily isolated intact and essentially free of contamination from other cells, organelles, and cytoplasmic contents. This membrane is complex enough to be interesting and, to some degree, representative, yet it is simple enough to be analyzed as a whole. These circumstances make it likely that the human red cell plasma membrane will be the first whose molecular anatomy is known in any degree of satisfying detail. The literature concerning the proteins of erythrocyte membranes and membranes in general has been the subject of repeated review (1 9). This article will focus on the localization and modes of association of individual major polypeptides within the human red cell membrane.