Showing papers on "Protein–protein interaction published in 1974"

X-Ray Studies of Protein Interactions

Abstract: INTRODUCTION 475 PROTEIN-PROTEIN INTERACTIONS 476 The Folding Problem 476 Secondary Structure 476 Tertiary Structure: A Tool in the Study of Evolution 482 Quaternary Structure 485 PROTEIN-METAL INTERACTIONS 489 General Observations 489 Functional Roles of Metal Ions in Proteins 489 Stabilization of structure and changes of conformation 489 Distorted metal coordination 491 PROTEIN-SOLVENT INTERACTIONS : 492 Interactions with Water 492 Structural results 492 Effect on folding 493 Interactions with Anions and Cations 494 Relationship Between Protein Structure in Solution and Crystal 495 PROTEIN-NUCLEIC ACID INTERACTIONS 496 DYNAMIC INTERACTIONS ; CATALYSIS ’ 497 Serine Proteinases 498 Substrate binding and catalysis 498 Substrate specificity 499 Structure-Function Relationship in Dehydrogenases 501 CONCLUSION 502

[75] Purification of proteins involved in Ca(II)-dependent protein-protein interactions (coagulant protein of Russell's viper venom)

Abstract: Publisher Summary The application of affinity chromatography to the purification of enzymes that catalyze reactions involving protein substrates has been limited until recently to proteases for which specific inhibitors or ligands are known. In the absence of the availability of highly specific inhibitors or synthetic substrates, an alternative chromatographic method is proposed for the purification of enzymes involved in Ca (II)-dependent protein–protein interactions. The interaction of trivalent lanthanide ions with the metal-binding sites of Ca (II)-binding proteins has been demonstrated for albumin, trypsinogen, amylase, thermolysin, staphylococcal nuclease, and bovine Factor X. Although the Ca (II) requirement of some enzymatic activities may be replaced by lanthanide ions, the lanthanide ions do not promote staphylococcal nuclease activity. Factor X is a circulating plasma zymogen which participates in an intermediate step of the blood coagulation cascade. In addition to physiological modes of activation, factor X may be activated by a coagulant protein in Russell's viper venom. The reaction of coagulant protein on factor X is proteolytic, has an absolute requirement for Ca (II), and proceeds at physiological pH.