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Chemical Modification of Proteins
2003The two most widely used applications for chemical modification are in primary structure analysis and in the identification of essential groups involved in the binding and catalytic sites of proteins. The methods discussed here are those used frequently in primary structure analysis.
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Covalent Modifications of G-Proteins
Annual Review of Pharmacology and Toxicology, 1993G-proteins . In addition , many membe rs of the G-prote in supe rf amil ie s are substrates for a large number of covalent modi fica ti ons . Among thes e are nearly every covalent modi fica ti on know n (with the exception of glyco syla ti on) , inclu di ng ADP-ribo syla tion , preny la tion, acyla tion , and phos phory la tion.
H K, Yamane, B K, Fung
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[56] Carbodiimide modification of proteins
1972A carbodiimide-nucleophile procedure for modifying carboxyl groups in proteins can be utilized under mild conditions for the quantitative determination of all carboxyl groups or for the modification of selected residues in activity studies. The method allows numerous variations both in the activating carbodiimide and in the nature of the nucleophile ...
K L, Carraway, D E, Koshland
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Analysis of Oxidative Modification of Proteins
Current Protocols in Protein Science, 2000AbstractProtein oxidation has been implicated in a variety of degenerative diseases as well as in the aging process. This unit describes techniques for the quantification of various protein oxidation products, including protein carbonyls, loss of protein thiol groups, dityrosine and nitrotyrosine, and isoaspartate formation.
L J, Yan, R S, Sohal
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Protein Modification and Autophagy Activation
2019Protein modification refers to the chemical modification of proteins after their biosynthesis, which is also called posttranslational modification (PTM). PTM causes changes in protein properties and functions. PTM includes an attachment of addition of functional groups, such as methylation, acetylation, glycosylation and phosphorylation; a covalent ...
Rui, Wang, Guanghui, Wang
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Kinetics of Amine Modification of Proteins
Bioconjugate Chemistry, 2006A simple kinetic model for coupling small molecules such as biotin to proteins with amine-reactive reagents such as N-hydroxysuccinimide esters is developed. It predicts the reagent concentration required to modify a protein at a given concentration to a specified number of modified amines per molecule.
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Lipid modification of G proteins
Trends in Cardiovascular Medicine, 1994The heterotrimeric guanine nucleotide-binding G proteins, composed of α, β, and γ subunits, act as signal transducers between cell surface receptors and downstream effector molecules, leading to changes in intracellular second messengers. The superfamily of ras-related low-molecular-mass GTP-binding G proteins is involved in a number of cellular ...
B T, Kinsella, D J, O'Mahony
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Cofactors in and as posttranslational protein modifications
The FASEB Journal, 1988A symposium at the FASEB meeting in Las Vegas in May 1988 will be devoted to the role of cofactors (vitamins, coenzymes, prosthetic groups) in and as posttranslational protein modifications; the symposium is part of a thematic focus on metabolic regulation.
R B, Rucker, F, Wold
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Posttranslational protein modifications
Critical Care Medicine, 2005Robert S B, Clark +2 more
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Oxidative modifications of protein structures
2001Publisher Summary This chapter discusses the oxidative modifications and biological effects of protein structures. Proteins undergo oxidative modifications due to the complexity of their chemical structures in subsequent stages which depend on the presence of oxidation, susceptible groups and on steric availability of these groups for oxidant attacks.
J W, Naskalski, G, Bartosz
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