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Thursday, November 5, 2020 | History

5 edition of Chemical modification of proteins found in the catalog.

Chemical modification of proteins

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Published by North-Holland Pub. Co., Sole distributors for the U.S.A. and Canada, American Elsevier Pub. Co. in Amsterdam, New York .
Written in English

    Subjects:
  • Proteins -- Analysis.,
  • Separation (Technology),
  • Nucleic acids -- Analysis.,
  • Nucleotides -- Analysis.

  • Edition Notes

    Includes bibliographies and indexes.

    Other titlesSeparation methods for nucleic acids and oligonucleotides.
    StatementA.N. Glazer, R.J. DeLange and D.S. Sigman. Separation methods for nucleic acids and oligonucleotides / Hannah Gould and H.R. Matthews.
    SeriesLaboratory techniques in biochemistry and molecular biology -- v. 4, pt. 1-2
    ContributionsDeLange, R. J., Sigman, D. S., Gould, Hannah., Matthews, Harry Roy, 1942-
    The Physical Object
    Paginationviii, 491 p. :
    Number of Pages491
    ID Numbers
    Open LibraryOL22119093M
    ISBN 100720442001, 072044215X

    Comprehensive and state-of-the-art, Posttranslational Modifications of Proteins: Tools for Functional Proteomics serves as a highly practical guide for all investigators of protein structure-function relationships not only in chemical and pharmaceutical research, but also throughout the rapidly growing field of functional proteomics.   Key Terms. Posttranslational modification: the chemical modification of a protein after its is one of the later steps in protein biosynthesis, and thus gene expression, for many proteins. translation: A process occurring in the ribosome, in which a strand of messenger RNA (mRNA) guides assembly of a sequence of amino acids to make a protein. The book begins by explaining how proteins are purified and describes methods for elucidating their sequences of amino acids and defining their posttranslational modifications. Comprehensive explanations of crystallography and of noncovalent forcesDLionic interactions, hydrogen bonding, and the hydrophobic effectDLact as a prelude to an. The word crosslinking implies durable combination of (usually large) distinct elements at specific places to create a new entity that has different properties as a result of the union. In the case of proteins, such crosslinking often results in important changes in chemical, functional.


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Chemical modification of proteins by Alexander N. Glazer Download PDF EPUB FB2

Chemical modification of an existing protein can be useful for probing structure, function and stability relationships of proteins. Chemical modification can serve as a replacement or complementary method to recombinant DNA technology for improving the properties of a protein (Table ).This may have particular benefit for proteins targeted for commercial exploitation due to the increasing.

Protein chemical modification is a problem-solving technique in research and technology. Modifications also occur in natural deteriorations. Generally these modifications are with the most reactive side chains and are predominantly oxidations, reductions, and nucleophilic and electrophilic substitutions.

Chemical modification in biochemistry. Main Article: [insert main article link] In biochemistry, chemical modification is the technique of anatomically reacting a protein or nucleic acid with a reagent or reagents. Obtaining laboratory information through chemical modification which can be utilized to.

Additional Physical Format: Online version: Means, Gary E. Chemical modification of proteins. San Francisco, Holden-Day [] (OCoLC) Document Type.

Chemical Modification of Proteins (Laboratory Techniques in Biochemistry & Molecular Biology) (Vol 4) 1st Edition by R. DeLange (Author), D. Sigman (Contributor) › Visit Amazon's D. Sigman Page. Find all the books, read about the author, and more. See search results for this author Cited by: Examining the chemical modification of biological polymers and the emerging applications of this technology, Chemical Modification of Biological Polymers reflects the change in emphasis in this subsection of biotechnology from the study of protein structure and function toward applications in therapeutics and diagnostics.

Highlights. The basic organic chemistry of the modification proteins Cited by: Chemical modification of proteins book. The Proteins, Third Edition, Volume II is a three-chapter text that highlights the application of methods of organic chemistry to the study of protein structure.

Chapter 1 reviews the chemical modification of proteins by group- and site-specific reagents. Book Description. The use of the chemical modification of proteins has evolved over the past 80 years, benefiting from advances in analytical, physical, and organic chemistry.

Over the past 30 years, the use of chemical reagents to modify proteins has been crucial in determining the function and structure of purified proteins. The chemical modification of proteins is an important tool for probing natural systems and synthesizing novel conjugates.

Here, Spicer and Davis review the merits and limitations of the most Cited by: ISBN: X OCLC Number: Description: viii, pages: illustrations ; 21 cm. First published inChemical Reagents for Protein Modification, 2nd Edition provides a unique combination of theoretical and practical considerations for the use of chemical reagents for site-specific modification of proteins.

The book is divided into three sections, with the Chemical modification of proteins book section describing general techniques, including Book Edition: 1st Edition. Purchase Chemical Modification of Proteins, Volume 4 - 1st Edition. Print Book & E-Book. ISBNBook Edition: 1. Protein Post-Translational Modification.

Protein modifications performed by “extra-translational” processes. Cannot be definitively predicted from DNA sequence. Can involve very complex systems of enzymes.

In some cases, “consensus” sites of modification can be identified. Ubiquitous in eukaryotes. Frequently critical for:File Size: KB. The deteriorative type includes the Maillard reaction and the alkaline degradations leading to compounds like lysinoalanine.

Although the intentional chemical modification of food proteins is currently applied to only a limited extent, it offers opportunities for improving food proteins and extending their availability from nonconventional sources.

The use of the chemical modification of proteins has evolved over the past 80 years, benefiting from advances in analytical, physical, and organic chemistry.

Over the past 30 years, the use of chemical reagents to modify proteins has been crucial in determining the function and structure of purified proteins.

This groundbreaking work is part of the. Introduction. The chemical modification of peptides or proteins prior to MS-analysis is generally carried out for any of three purposes: (1) to attach an affinity handle to purify a subset of the proteome, (2) to incorporate stable isotope labels for relative quantification of two or more samples, and/or (3) to modify the physiochemical properties of peptides and proteins to improve them as Cited by: 7.

Unlike chemical modification of residues, which often is reversible, processing of some proteins causes irreversible changes that alter their activity.

In the most common form of processing, residues are removed from the C- or N-terminus of a polypeptide by cleavage of the peptide bond in a reaction catalyzed by by: 1.

Offers discussions on the chemical and physicochemical modification of proteins for the enhancement of surface activity and functional properties in a variety of systems.

The volume provides examples of specific applications of modified proteins in gelation, emulsification, foaming, adsorption and surface tension reduction for use in the food Cited by: Book Description. Examining the chemical modification of biological polymers and the emerging applications of this technology, Chemical Modification of Biological Polymers reflects the change in emphasis in this subsection of biotechnology from the study of protein structure and function toward applications in therapeutics and diagnostics.

Highlights. The book places emphasis on conditions that affect the specificity of the chemical modification of proteins, such as solvent and temperature. The format has been markedly revised, presenting information based on the chemical nature of the modifying material and on the amino acid residue modified.

Regulation of Protein Surfaces Through Posttranslational Modification. Cite this entry as: () Chemical Modification of Proteins. In: Roberts G.C.K. (eds) Encyclopedia of Biophysics. First published inChemical Reagents for Protein Modification, 2nd Edition provides a unique combination of theoretical and practical considerations for the use of chemical reagents for site-specific modification of proteins.

The book is divided into three sections, with the first section desc. Post-translational modification (PTM) refers to the covalent and generally enzymatic modification of proteins following protein ns are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo PTM to form the mature protein product.

PTMs are important components in cell signaling, as for example when prohormones are converted to hormones. Chemical modification of proteins is an important tool for probing natural systems, creating therapeutic conjugates and generating novel protein constructs. The 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 by:   Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an encyclopedic work describing the many approaches to the site-specific modification of proteins.

More than 2, references are cited describing the development of the various reagents. This book Price: $   Selective chemical modification of proteins is enormously useful in a wide range of biological researches, including preparation of protein‐based pharmaceuticals, posttranslational modifications of proteins, visualization of protein activity, modulation of protein function in live cells, and affinity‐based protein : Xi Chen, Stephanie Voss, Yao‐Wen Wu.

In later years, mechanisms of chemical modification of proteins by ROS/RNS were investigated until the s, notably by E.R. Stadtman, R.L. Levine, R.T. Dean, K.J. Davies, and others, and were. Therefore, chemical modification with small molecules has attracted much attention as an alternative protein modification technology.

In this chapter, several key bioconjugation reactions leading to non-specific chemical modifications and the recent amino acid residue-specific chemical modifications of proteins are first summarized in Sect.

: Hiroyuki Nakamura. Chemical Modification of Proteins. Gary E. Means, Robert Earl Feeney. Holden-Day, - Organic compounds - pages. 0 Reviews. From inside the book. What people are saying - Write a review. We haven't found any reviews in the usual places.

Contents. MODIFICATIONS TO CHANGE PROPERTIES. "Christopher Walsh, an acclaimed scientist, has written yet another outstanding book. It surveys the vast field of chemical modifications that proteins undergo in living cells.

The book's depth of coverage and clarity of exposition will make it an indispensable text for both students and active researchers.". Processing also alters food proteins. Thermal processing is the common and traditional method of processing foods.

However, nonthermal processes such as high pressure and pulsed electric field processing have been of interest recently. This chapter reviews denaturation, chemical modification of food proteins as well as processing‐induced by: 4. Aim: The aim of the present study was to assess the influence of the chemical characteristics and roughness of titanium surfaces on the viability, proliferation and differentiation of osteoblast-like cells cultured in a medium supplemented with recombinant human bone morphogenetic protein-7 (rhBMP-7).

Material and methods: Osteo-1 cells were grown on titanium disks presenting with the. Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis C.

Ryan, books or book chapters) do not need to formally request Cited by: Chemical modification of biological polymers Roger L Lundblad. Language: english. Pages: ISBN proteins protein acid chem residues groups amino chemical cysteine You can write a book review and share your experiences.

Other readers will always be interested in your. DOI: /asia Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology Justin M. Chalker, GonÅalo J. Bernardes, Yuya A. Lin, and Benjamin G. Davis*[a] Wiley-VCH Verlag GmbH&Co.

KGaA, Weinheim Chem. Asian J. Most chemical modifications made to proteins within cells occur after the protein is synthesized in a process called translation. The resulting chemical changes are termed post-translational modifications.

Figure: Post-translational modification of proteins. Here is a list of post-translational modification from the Swiss Institute of. Modification involves attaching or cleaving chemical groups to alter the solubility or other properties of the original molecule.

"Labeling" generally refers to any form of crosslinking or modification whose purpose is to attach a chemical group (e.g., a fluorescent molecule) to aid in detection of a molecule and is described in other articles. This exciting laboratory support book encompasses the encyclopedic coverage of the most frequently used methods for the site-specific chemical modification of proteins.

In a concise manner, it presents methods for the characterization of modified proteins, including: amino acid analysis protein sequence analysis chemical cleavage of protein. Modification reagents for proteins and peptides are chemical agents that are used to modify the amino acid side chains in order to alter the native charges, block or expose reactive binding sites, inactivate functional groups, and change functional groups to create targets for crosslinking and labeling.

Proteins come in various sizes and shapes. Those with thread-like shapes, the fibrous proteins, tend to have structural or mechanical roles.

Those with spherical shapes, the globular proteins, function as enzymes, transport proteins, or antibodies. Fibrous proteins tend to be water-insoluble, while globular proteins tend to be Size: 2MB.8 Chemoselective Modification of Proteins Xi Chen, Stephanie Voss, and Yao-Wen Wu.

Chemical Protein Synthesis Chemoselective and Bioorthogonal Reactions Site-Selective Protein Modification Approaches References 9 Stable, Versatile Conjugation Chemistries for Modifying Aldehyde-Containing Biomolecules Covering: up to February Identification of the target proteins of natural products is pivotal to understanding the mechanisms of action to develop natural products for use as molecular probes and potential therapeutic drugs.

Affinity chromatography of immobilized natural products has been conventi Strategies for Cellular Target Identification of Natural Products.