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2 edition of Crystallographic studies of carbohydrate modifying proteins found in the catalog.

Crystallographic studies of carbohydrate modifying proteins

Valerie Notenboom

Crystallographic studies of carbohydrate modifying proteins

mechanisms of action in plysaccharide binding and catalysis.

by Valerie Notenboom

  • 27 Want to read
  • 8 Currently reading

Published .
Written in English


The Physical Object
Pagination200 leaves.
Number of Pages200
ID Numbers
Open LibraryOL20049406M
ISBN 100612499359

Proteins formed by a linear combination of amino acids monomers (among 20) by peptide linkage Carbohydrates formed by linear or branched combination of monosaccharides monomers by glycosidic linkage Lipids form large structures but the interactions are . Carbohydrate-binding proteins can interact with sugars but do not modify them, and play a pivotal role in a variety of important biological recognition processes. Most studies predict carbohydrate-binding sites, but not carbohydrate-binding proteins. The existing method of .


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Crystallographic studies of carbohydrate modifying proteins by Valerie Notenboom Download PDF EPUB FB2

Crystallographic Studies of Carbohydrate Modifying Proteins: Mechanisms of Action in Polysaccharide Binding and Catalysis Doctor of Philosophy Vaierie Notenboom Department of Medicai Biophysics University of Toronto Abstract Enzymatic degradation of cellulose and.

X-ray crystallographic studies of At g proteins involved in ubiquitin-like conjugation reactions Of the 18 Atg proteins essential for autophag osome formation, eight, namely, Atg3, Atg4. from book Fibrous Proteins: Structures and Mechanisms (pp) Crystallographic Studies of Intermediate Filament Proteins.

Chapter January The mode of binding of oligosaccharides to griffithsin, an antiviral lectin from the red alga Griffithsia sp., was investigated by a combination of X‐ray crystallography, isothermal titration calorimetry, and molecular modeling.

The structures of complexes of griffithsin with 1→6α‐mannobiose and with maltose were solved and refined at the resolution of and Å, respectively.

Crystallographic Studies on Autophagy-Related Proteins. By Nobuo N. Noda, Yoshinori Ohsumi and Fuyuhiko Inagaki. Submitted: March 9th Reviewed: September 5th Published: December 16th DOI: /Author: Nobuo N.

Noda, Yoshinori Ohsumi, Fuyuhiko Inagaki. Acta Crystallogr F Struct Biol Commun. Aug;71(Pt 8) doi: /SX Epub Jul Purification and crystallographic studies of a putative carbohydrate-binding module from the Ruminococcus flavefaciens FD-1 endoglucanase : Ana José Pires, Teresa Ribeiro, Andrew Thompson, Immacolata Venditto, Vânia O.

Fernandes, Pedro Bule. Intermediate filaments (IFs), together with microtubules and actin microfilaments, are the three main cytoskeletal components in metazoan cells. IFs are formed by a distinct protein family, which is made up of 70 members in humans.

Most IF proteins are tissue- or organelle-specific, which includes lamins, the IF proteins of the by:   Goals / Objectives The objectives of this study are to determine the structure and function of proteins with the crystallographic methods.

The current focus of the laboratory is on four major areas. understanding the molecular basis of motility. understanding how enzymes evolve through the reuse of structural and catalytic frameworks.

ADVERTISEMENTS: In this article we will discuss about the X-ray crystallographic studies of DNA. Inthe basic chemical composition of nucleic acid was elucidated through the efforts of P.A.

Levene. Infor the first time W.T. Astbury gave first three dimensional structure of DNA model studied through X-ray crystallography. He concluded that its [ ]. Effects of temperature on protein structure and dynamics: x-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to K.

Robert F. Tilton, Jr. John C. Dewan; Gregory A. PetskoCited by: past and present contribution of crystallographic studies as a guide to functional understanding, with a final look towards the future. Discovery of LMPOs and initial structural and functional studies Setting the scene: enzymes breaking glycosidic linkages.

Crystallographic studies of the complex of human HINT1 protein with a non-hydrolyzable analog of Ap4A. Dolot R(1), Kaczmarek R(2), Sęda A(2), Krakowiak A(2), Baraniak J(2), Nawrot B(2).

Author information: (1)Department of Bioorganic Chemistry, Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, SienkiewiczaCited by: 6.

Exponential growth in the number of patients suffering from diseases caused by the consumption of sugar has become a threat to mankind's health. Artificial low calorie sweeteners available in the market may have severe side effects.

It takes time to figure out the long term side effects and by the time these are established, they are replaced by a new low calorie sweetener. Studies on proteins that develop 3D domain swapping might provide some clues on the early stages of amyloid formation. The SH3 domain is a small modular domain that has been used as a model to study the basis of protein by: 4.

The presented HINT1/JB complex structure is the first one of the HINT1 protein in a complex with a ligand other than a nucleoside, a mononucleotide or their analog. In addition, for comparative studies, the apo HINT1 structure crystallized in P2 1 space group is Cited by: 6.

Crystallographic, Thermodynamic, and Molecular Modeling Studies of the Mode of Binding of Oligosaccharides to the Potent Antiviral Protein Griffithsin Natasza E. Zio´łkowska,1 Shilpa R. Shenoy,2 Barry R. O’Keefe, 3James B. McMahon, Kenneth E. Palmer,4 Raymond A.

Dwek, 5Mark R. Wormald, and Alexander Wlodawer1*. Crystallization and preliminary X-ray crystallographic studies of the ice-binding protein from the Antarctic yeast Leucosporidium sp. AY Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67 (7), Cited by: 4.

Abstract. In recent years several symposia and conferences have focused upon the topic of biological recognition, particuarly as it applies to protein-nucleic acid systems (Eisenberg et al., ; Parsegian, ; Vogel, ; Sarma,).Attempts have been made to delineate the atomic interactions by which these macromolecules recognise and bind to one another, since such knowledge Cited by: 1.

Ribosomal proteins are a major component of ribosomes, which catalyze protein synthesis. One ribosomal protein, L7a (RPL7a), which is a component of the 60S large ribosomal subunit, has additional functions involved in cell growth and differentiation that occur via interaction with human thyroid hormone receptor (THR) and retinoic acid receptor (RAR) and in turn inhibit the activities of the Cited by: 2.

Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine NATASZA E. ZIO´ ŁKOWSKA,1 SHILPA R. SHENOY,2 BARRY R. O’KEEFE,3 AND ALEXANDER WLODAWER 1 1Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI-Frederick, Frederick, Maryland G protein–coupled receptors (GPCRs) are integral membrane proteins that respond to environmental signals and initiate signal transduction pathways activating cellular processes.

Rhodopsin is a GPCR found in rod cells in retina where it functions as a photopigment. Its molecular structure is known from cryo-electron microscopic and X-ray crystallographic studies, and this has reshaped many. "A useful source." (Choice)"It is gratifying to see such a nice piece of work and the book is highly recommended." (Eddie Snell Reflexions: Newsletter of the American Crystallographic Association) "One of the main assets of the book is its many by: Title: Structural and Molecular Basis of Carbohydrate-Protein Interaction Systems as Potential Therapeutic Targets VOLUME: 17 ISSUE: 17 Author(s):Yukiko Kamiya, Maho Yagi-Utsumi, Hirokazu Yagi and Koichi Kato Affiliation:Okazaki Institute for Integrative Bioscience and Institute for Molecular Science, National Institutes of Natural Sciences, Higashiyama, Myodaiji, Okazaki, Aichi Learn chemistry carbohydrates proteins lipids with free interactive flashcards.

Choose from different sets of chemistry carbohydrates proteins lipids flashcards on Quizlet. Biochemical and X-ray crystallographic studies on shikimate kinase: The important structural role of the P-loop lysine TINO KRELL,1,6,7 JOHN MACLEAN,2,6,8 DEBORAH J. BOAM,1 ALAN COOPER,2 MARINA RESMINI,3 KEITH BROCKLEHURST,4 SHARON M.

KELLY,5 NICHOLAS C. PRICE,5 ADRIAN J. LAPTHORN,2 AND JOHN R. COGGINS1 1Division of Biochemistry and Molecular. Carbohydrate–protein interactions are the intermolecular and intramolecular interactions between protein and carbohydrate moieties.

These interactions form the basis of specific recognition of carbohydrates by lectins. Carbohydrates are important biopolymers and have a variety of functions. Often carbohydrates serve a function as a recognition element. Occurs with its polymer chain extended in fibrous proteins, or coiled into a compact macromolecule in enzymes and other globular proteins.

The component amino acids are encoded in the triplets of messenger RNA, and proteins are the products of genes a carbohydrate made up of two monosaccharides (simple sugars). Oligosaccharides. a polymer. The X‐ray structure of an oxygenated hemocyanin molecule, subunit II of Limulus polyphemus hemocyanin, was determined at Å resolution and refined to a crystallographic R‐factor of %.The 73‐kDa subunit crystallizes with the symmetry of the space group R32 with one subunit per asymmetric unit forming hexamers with 32 point group symmetry.

onscreen. Crystallographic modeling at the computer interface is thus not only a means of producing representations of proteins; it is also means of training novice crystallographers’ bodies and imaginations.

Protein crystallographers’ molecular embodiments thus offer a site for posing a new range of questions for studies of the visual cultures. X-ray Crystallographic Studies on the Noncovalent Syntheses of Supermolecules Matthew C T Fyfe, J.

Fraser Stoddart *, David J. Williams * Corresponding author for this workCited by: : Crystallographic and Metacrystallographic Groups (): Opechowski, W.: BooksCited by: Biological macromolecules like proteins, lipids (fats), and carbohydrates (sugars and starches) are the building blocks of living cells.

Home Biology: Food Labs (Biochemistry) What You Should Know – Carbohydrate Foods Honors Biology--More complex macromolecule. Numerous key discoveries in biology have emerged from studies of RNA (ribonucleic acid), including seminal work in the fields of biochemistry, genetics, microbiology, molecular biology, molecular evolution and structural of30 scientists have been awarded Nobel Prizes for experimental work that includes studies of RNA.

Specific discoveries of high biological significance are. The primary method to obtain information on disordered regions of a protein is NMR spectroscopy. The lack of electron density in X-ray crystallographic studies may also be a sign of disorder. Folded proteins have a high density (partial specific volume of.

Edward R.T. Tiekink had a brief stint at NUS () before joining the University of Texas at San Antonio in the Fall of While at NUS his research interests revolved around chemical crystallography with an emphasis on main group element chemistry, the development of metal-based drugs for the treatment of cancer, rheumatoid arthritis and tropical diseases and new molecular materials.

For a good understanding, it will help you to look a biochemistry text book chapters on lipids and carbohydrates. Briefly: 1.

Both lipid and carbohydrate groups are composed of many types of molecules that differ from very small to very large. Order Parameters and Crystallographic B-factors for a Small a/b Protein: A Unified Picture of High Probability, Fast Atomic Motions in Proteins G. Marius Clore1* and Charles D.

Schwieters2* 1LaboratoryofChemicalPhysics Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda MD File Size: KB. Crystallographic studies on a cold adapted subtilase and proteins involved in mRNA processing Dissertation zur Erlangung des Doktorgrades der Mathematisch-Naturwissenschaftlichen Fakultäten der Georg-August-Universität zu Göttingen vorgelegt von Jóhanna Arnórsdóttir aus Reykjavík Göttingen n Studies of carbohydrate-protein interaction by capillary electrophoresis A.

Tag a, S. Y asueda, M. Mochizuki, H. Itoh and S. Honda F aculty of Pharmaceutical Sciences, Kinki University, Kow akae, Higashi-osakaJa pan Capillary electrophoresis is a useful tool for esti - mation of the binding constant between small.

Cellulosomes, Cellulases & Other Carbohydrate Modifying Enzymes Gordon Research Conference AugustProctor Academy, Andover NH, USA, Conference Proceedings P24 (session II), p. Subsequently, protein ligands were introduced as specific binders for Nkrp1 proteins and three dimensional models of receptor/protein ligand interaction were derived from crystallographic data.

Finally, for at least some members of the NK cell C-type lectin-like proteins, the “sweet story” was impaired by two reports in recent years.THE JOURNAL OF BIOLOGICAL CHEMISTRY Q by The American Society for Biochemistry and Molecular Biology, Inc.

Vol.No. 31, Issue of November 5, pp, Physical Characterization and Crystallization of the Carbohydrate- recognition Domain of a Mannose-binding Protein from Rat* (Received for publication, J) William I. WeisSO, Gregg V. Crichlow, H. M. Krishna.

Also, as already mentioned for other cations, there is no ruthenium bound at the a priori equivalent site related by non‐crystallographic symmetry in the subtype‐B duplex.

Cobalt(III) hexammine is commonly used as a probe replacing hexahydrated Cited by: