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Jack Kyte

Researcher at University of California, San Diego

Publications -  21
Citations -  22703

Jack Kyte is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Trypsin & Enzyme. The author has an hindex of 13, co-authored 21 publications receiving 21851 citations. Previous affiliations of Jack Kyte include Albert Einstein College of Medicine & University of California, Los Angeles.

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A simple method for displaying the hydropathic character of a protein

TL;DR: A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.
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Molecular considerations relevant to the mechanism of active transport.

TL;DR: It is now known that systematic errors were responsible for this mistaken conclusion that ‘half-of-sites’ behaviour, consistent with this hypothesis, has been reported, and the number of protomers which comprise a functional unit of active transport has not been determined.
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Human erythrocyte calmodulin. Further chemical characterization and the site of its interaction with the membrane.

TL;DR: Calmodulin stimulates calcium-activated adenosine triphosphatase by a simple enzyme-ligand association and human erythrocyte and bovine brain calmodulins were indistinguishable by tryptic peptide mapping, indicating that the primary sequence of the two proteins is either very similar or identical.
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The Reactions of Sodium and Potassium Ion-activated Adenosine Triphosphatase with Specific Antibodies IMPLICATIONS FOR THE MECHANISM OF ACTIVE TRANSPORT

TL;DR: The experiments demonstrate that the antigenic sites on the large subunit, recognized by the anti-large chain antibody, are located only on the inner surface of the plasma membrane in the intact cell, and therefore rule out any diffusional carrier mechanism for the active transport of alkali metal ions.
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Dimerization of the Extracellular Domain of the Receptor for Epidermal Growth Factor Containing the Membrane-spanning Segment in Response to Treatment with Epidermal Growth Factor

TL;DR: A recombinant fragment of the human receptor for epidermal growth factor containing both its extracellular domain and its membrane-spanning segment, when dissolved with Triton X-100, was observed to dimerize in response to addition of EGF even at the lowest concentration that could be assayed, suggesting that interfaces between cytoplasmic domains of intact EGF receptor impart significant stabilization to the dimer of the enzyme.