Limited proteolysis in microorganisms
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Limited proteolysis in microorganisms biological function, use in protein structural and functional studies : a conference by International Conference on Limited Proteolysis in Microorganisms (1978 National Institutes of Health)

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Published by U.S. Dept. of Health, Education, and Welfare in [Washington] .
Written in English

Subjects:

  • Proteolytic enzymes -- Congresses.,
  • Microbial enzymes -- Congresses.

Book details:

Edition Notes

Includes bibliographies and index.

Statementsponsored by the National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institute of Allergy and Infectious Diseases, the John E. Fogarty International Center for Advanced Study in the Health Sciences, [at the] National Institutes of Health, Bethesda, Maryland, April 17-19, 1978 ; Georges N. Cohen, Helmut Holzer, editors.
SeriesDHEW publication ; no. (NIH) 79-1591, DHEW publication ;, no. (NIH) 79-1591.
ContributionsCohen, Georges N., Holzer, Helmut, 1921-, National Institute of Arthritis, Metabolism, and Digestive Diseases (U.S.), National Institute of Allergy and Infectious Diseases (U.S.), John E. Fogarty International Center for Advanced Study in the Health Sciences.
Classifications
LC ClassificationsQP609.P78 I55 1978
The Physical Object
Paginationvii, 255 p. :
Number of Pages255
ID Numbers
Open LibraryOL4372948M
LC Control Number78600168

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Regulated Proteolysis in Microorganisms (Subcellular Biochemistry Book 66) - Kindle edition by Dougan, David A.. Download it once and read it on your Kindle device, PC, phones or tablets. Use features like bookmarks, note taking and highlighting while reading Regulated Proteolysis in Microorganisms (Subcellular Biochemistry Book 66).Manufacturer: Springer. The item Limited proteolysis in microorganisms: biological function, use in protein structural and functional studies, Georges N. Cohen, Helmut Holzer, editors represents a specific, individual, material embodiment of a distinct intellectual or artistic creation found in Indiana State Library. Limited proteolysis is a simple biochemical method which can support information regarding protein structure, conformational changes (1 & 2). The principle of limited proteolysis is that a protein is incubated with a relatively low concentration of different proteases, which cut at recognition sites throughout the protein, normally at exposed. Get this from a library! Limited proteolysis in microorganisms: biological function, use in protein structural and functional studies. [Georges N Cohen; Helmut Holzer; National Institute of Allergy and Infectious Diseases (U.S.); National Institute of Arthritis, Metabolism, and Digestive Diseases (U.S.); John E. Fogarty International Center for Advanced Study in the Health Sciences.;].

Abstract. Proteolytic enzymes (or proteases, peptidases, or proteinases) hydrolyze the peptide bond in proteins and peptides. The nomenclature is imprecise, but there is a broad acceptance that endopeptidases break bonds that are “internal” in the primary sequences, whereas exopeptidases trim one, two, or perhaps three amino acids from the amino or carboxy Cited by: 7. A. Varshavsky, in Encyclopedia of Genetics, Proteolysis, or protein degradation is a set of processes that result in the hydrolysis of one or more of the peptide bonds in a protein, either through catalysis by proteolytic enzymes called proteases or nonenzymatically, for example at very low or very high living organisms, proteolysis is a part of protein turnover, in which . Accumulating evidence suggests that the cyclooxygenase-2 (COX-2) enzyme has additional catalytic-independent functions. Here we show that COX-2 appears to be cleaved in mouse and human tumors, which led us to hypothesize that COX-2 proteolysis may play a role in cell proliferation. The data presented herein show that a KR point mutation at the carboxyl . Proteolysis in hyperthermophilic bacteria is poorly understood, despite the availability of complete genomic sequences for T. maritima (Nelson et al. ) and A. aeolicus (Deckert et al. ). To date, only two proteases (Hicks et al. , Choi et al. ) and a leucine aminopeptidase (Khan et al. ) have been characterized Cited by:

In our research, we applied limited chymotrypsin proteolysis to propel the crystallization of the minor pseudopilin ternary complex of XcpVWX. Conspicuously, it is found that the crystal lattice formation and the resulting protein packing are correlated to the quantity of the protease and the duration of digestion used in the : Yichen Zhang, Shu Wang, Zongchao Jia. Learn proteolysis with free interactive flashcards. Choose from 95 different sets of proteolysis flashcards on Quizlet.   Regulation by proteolysis has been shown to be involved in diverse bacterial cellular processes including growth, division, differentiation, pathogenesis and stress response. This review will focus on the structure, degradation process, and the function of AAA + proteolytic machines in : Li S, Yao Y. Some possibilities for the control of proteolysis, which are supported by experimental findings in microorganisms and tissues from higher animals, have been presented and discussed by Goldberg and co-workers in recent reviews (5, 6). In this chapter possible control mechanisms of intracellular proteolysis in yeast will be by: 2.