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Relevant bibliographies by topics / Tryptophan residue

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Academic literature on the topic 'Tryptophan residue'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 February 2022

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Journal articles on the topic "Tryptophan residue"

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Strøm, Morten B., Bengt Erik Haug, Øystein Rekdal, Merete L. Skar, Wenche Stensen, and John S. Svendsen. "Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity." Biochemistry and Cell Biology 80, no. 1 (2002): 65–74. http://dx.doi.org/10.1139/o01-236.

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This review focuses on important structural features affecting the antimicrobial activity of 15-residue derivatives of lactoferricins. Our investigations are based on an alanine-scan of a 15-residue bovine lactoferricin derivative that revealed the absolute necessity of two tryptophan residues for antimicrobial activity. This "tryptophan-effect" was further explored in homologous derivatives of human, caprine, and porcine lactoferricins by the incorporation of one additional tryptophan residue, and by increasing the content of tryptophan in the bovine derivative to five residues. Most of the r

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Bruch, Thomas vom, and Klaus-Heinrich Röhm. "Fluorescence Properties of Hog Kidney Aminoacylase I." Zeitschrift für Naturforschung C 43, no. 9-10 (1988): 671–78. http://dx.doi.org/10.1515/znc-1988-9-1008.

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Abstract The state of the tryptophan residues of porcine kidney aminoacylase I (EC 3.5.1.14) was investigated by fluorescence spectroscopy and chemical modification. The pH-dependence of the fluorescence emission spectrum of the enzyme indicates that its native conformation prevails between pH 6 and 9.5. Within this range, the ionization of a residue with an apparent pKa of 7.1 quenches the enzyme fluorescence by about 15%. A similar reduction of fluorescence intensity accompanies the inactivation of aminoacylase I by treatment with N-bromosuccinimide in low excess. This suggests that in both

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Okada, Masahiro, Tomotoshi Sugita, and Ikuro Abe. "Posttranslational isoprenylation of tryptophan in bacteria." Beilstein Journal of Organic Chemistry 13 (February 22, 2017): 338–46. http://dx.doi.org/10.3762/bjoc.13.37.

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Posttranslational isoprenylation is generally recognized as a universal modification of the cysteine residues in peptides and the thiol groups of proteins in eukaryotes. In contrast, the Bacillus quorum sensing peptide pheromone, the ComX pheromone, possesses a posttranslationally modified tryptophan residue, and the tryptophan residue is isoprenylated with either a geranyl or farnesyl group at the gamma position to form a tricyclic skeleton that bears a newly formed pyrrolidine, similar to proline. The post-translational dimethylallylation of two tryptophan residues of a cyclic peptide, kawag

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Kuo, Soong Yu, May Whei Lin, Shih Sheng Jiang, Shu Hsien Hung, Chi Meng Tzeng, and Rong Long Pan. "A tryptophan residue involved in the inhibition of plant vacuolar H+-ATPase by 2-hydroxy-5-nitrobenzyl bromide." Functional Plant Biology 25, no. 6 (1998): 679. http://dx.doi.org/10.1071/pp98008.

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Treatment of the vacuolar H+ -ATPase from mung bean seedlings (Vigna radiata L.) with the tryptophan modifying agent 2-hydroxyl-5-nitrobenzyl bromide (HNBB), caused a progressive decline of the ATP hydrolysis activity and proton translocation in a time- and concentration-dependent manner. Dithiothreitol could not restore the inhibition of H+ -ATPase by HNBB, indicating possible involvement tryptophan, and not cysteine residues. Protection studies suggested that modified sites might not locate in the active domain. Kinetic analysis shows that Vmax but not Km of H+ -ATPase was changed by HNBB. T

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Sarkar, Sayani, Adaitya Prasad Behera, Prateeka Borar, Prerana Agarwal Banka, and Ajit B. Datta. "Designing active RNF4 monomers by introducing a tryptophan: avidity towards E2∼Ub conjugates dictates the activity of ubiquitin RING E3 ligases." Biochemical Journal 476, no. 10 (2019): 1465–82. http://dx.doi.org/10.1042/bcj20180883.

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Abstract Ubiquitin RING E3 ligases (E3s) catalyze ubiquitin (Ub) transfer to their substrates by engaging E2∼Ub intermediates with the help of their RING domains. Different E3s have been found to contain a conserved tryptophan residue in their RING that plays an essential role in E2 binding and, hence, enzymatic activity. Many active E3s, however, lack this specific residue. We mined through the existing data to observe that the conservation of the tryptophan and quaternary organization of the RING domains are remarkably correlated. Monomeric RINGs possess the tryptophan while all well-charact

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Dementieva, Ekaterina I., Elena A. Fedorchuk, Lubov Yu Brovko, Alexander P. Savitskii, and Natalya N. Ugarova. "Fluorescent Properties of Firefly Luciferases and Their Complexes with Luciferin." Bioscience Reports 20, no. 1 (2000): 21–30. http://dx.doi.org/10.1023/a:1005579016387.

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Fluorescence of luciferases from Luciola mingrelica (single tryptophanresidue, Trp-419) and Photinus pyralis (two tryptophan residues, Trp-417,Trp-426) was studied. Analysis of quenching of tryptophan fluorescenceshowed that the tryptophan residue conserved in all luciferases is notaccessible for charged quenchers, which is explained by the presence ofpositively and negatively charged amino acid residues in the close vicinityto it. An effective energy transfer from tryptophan to luciferin wasobserved during quenching of tryptophan fluorescence of both luciferaseswith luciferin. From the data o

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MALOVRH, Petra, Ariana BARLIĆ, Zdravko PODLESEK, Peter MAĆEK, Gianfranco MENESTRINA, and Gregor ANDERLUH. "Structure–function studies of tryptophan mutants of equinatoxin II, a sea anemone pore-forming protein." Biochemical Journal 346, no. 1 (2000): 223–32. http://dx.doi.org/10.1042/bj3460223.

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Equinatoxin II (EqtII) is a eukaryotic cytolytic toxin that avidly creates pores in natural and model lipid membranes. It contains five tryptophan residues in three different regions of the molecule. In order to study its interaction with the lipid membranes, three tryptophan mutants, EqtII Trp45, EqtII Trp116/117 and EqtII Trp149, were prepared in an Escherichia coli expression system [here, the tryptophan mutants are classified according to the position of the remaining tryptophan residue(s) in each mutated protein]. They all possess a single intrinsic fluorescent centre. All mutants were le

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Friedman, M. L., K. T. Schlueter, T. L. Kirley, and H. B. Halsall. "Fluorescence quenching of human orosomucoid. Accessibility to drugs and small quenching agents." Biochemical Journal 232, no. 3 (1985): 863–67. http://dx.doi.org/10.1042/bj2320863.

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The fluorescence behaviour of human orosomucoid was investigated. The intrinsic fluorescence was more accessible to acrylamide than to the slightly larger succinimide, indicating limited accessibility to part of the tryptophan population. Although I- showed almost no quenching, that of Cs+ was enhanced, and suggested a region of negative charge proximal to an emitting tryptophan residue. Removal of more than 90% of sialic acid from the glycan chains led to no change in the Cs+, I-, succinimide or acrylamide quenching, indicating that the negatively charged region originates with the protein co

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Swamy, Musti Joginadha, and Avadhesha Surolia. "Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding." Bioscience Reports 9, no. 2 (1989): 189–98. http://dx.doi.org/10.1007/bf01115995.

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Modification of tryptophan side chains of soybean agglutinin (SBA) with N-bromosuccinimide results in a loss of the hemagglutinating and carbohydrate binding activities of the protein. One residue/subunit is probably essential for the binding activity. Modification leads to a large decrease in the fluorescene of the protein accompained by a blue shift. Iodide ion quenching of the protein fluorescence shows that saccharide binding results in a decreased accessibility of some of the tryptophan side chains. These results strongly point towards the involvement of tryptophan residues in the active

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Zhang, Z., K. Ostanin, and R. L. Van Etten. "Covalent modification and site-directed mutagenesis of an active site tryptophan of human prostatic acid phosphatase." Acta Biochimica Polonica 44, no. 4 (1997): 659–72. http://dx.doi.org/10.18388/abp.1997_4368.

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Because tryptophans are found as part of the phosphate binding sites in a number of proteins, human prostatic acid phosphatase (hPAP) was examined for the presence and the role of essential tryptophan residues. The pH dependence of the intrinsic fluorescence of hPAP resembled the kinetic pH dependence. Chemical modification by N-bromosuccinimide (NBS) resulted in an inactivation of the enzyme and produced a characteristic reduction of the protein absorbance at 280 nm. Two tryptophans per subunit were modified, and this was accompanied by an apparently complete loss of enzymatic activity. In th

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Dissertations / Theses on the topic "Tryptophan residue"

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McAllister, Kelly Ann. "Identification of a tryptophan residue in the active site of catalytic domain B of xylanase C from Fibrobacter succinogenes S85." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ27522.pdf.

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Jaquith, James B. "Synthesis of Angiotensin-converting Enzyme, ACE, inhibitors using dynamic kinetic resolution, Synthesis of the highly methylated tryptophan residue of hemiasterlin using glycidic ester ring opening reactions ; Synthesis of benz(o)indenes." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0019/NQ46525.pdf.

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Gross, Martin. "The tryptophan residues of mitochondrial creatine kinase : roles in enzyme structure and function /." [S.l.] : [s.n.], 1994. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=10719.

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Herron, Lissa. "Determining Which Tryptophan Residues Give Rise to Fluorescence Properties in the Metallo-Beta-Lactamase L1." Miami University Honors Theses / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=muhonors1110916836.

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Röjdeby, Elin. "Thermostability investigation of Fatty Acid Binding Protein from Cataglyphis fortis by fluorescence spectroscopy using genetically introduced tryptophan residues." Thesis, Linköpings universitet, Institutionen för fysik, kemi och biologi, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-74238.

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The desert ant Cataglyphis fortis is one of the hyperthermophilic species of Cataglyphis. It lives in the Sahara desert and forages during the hottest hours of the day when it can get up to 70˚C in the sand. The body temperature of the ant during the foraging runs can reach a maximum of 55˚C. Since C.fortis is one of few eukaryotic hyperthermophilic species, its proteins probably have a high thermostability. Investigating the thermostability can give valuable information about the principles of protein folding and stability in hyperthermophiles.Fatty acid binding proteins (FABPs) have an impor

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Mendive, Tapia Lorena. "Indole arylation in tryptophan residues: development of new chemical methodologies, synthetic studies and biological evaluation of modified peptides." Doctoral thesis, Universitat de Barcelona, 2017. http://hdl.handle.net/10803/401593.

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In the present thesis we have investigated the development of new methodologies for the selective and straightforward chemical modification of Trp amino acid either alone or in peptides. In the first chapter, we have optimized a method for the chemoselective C-arylation of Trp amino acid in the C-2 position of the free indole ring, based on a C-H activation protocol catalyzed by palladium. To further demonstrate the versatility of the protocol, indoles from tryptamines, indole- carboxylic acids, Trp amino acid and Trp-containing peptides (e.g. Brevianamide F) were selectively arylated. In p

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Schafheimer, Nathaniel (Steven Nathaniel). "Ultraviolet radiation-induced aggregation of human lens protein [g̳a̳m̳m̳a̳]D-crystallin : characterization of the protective tryptophan clusters and key sensitizing residues." Thesis, Massachusetts Institute of Technology, 2013. http://hdl.handle.net/1721.1/83640.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2013.<br>This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections.<br>Cataloged from student-submitted PDF version of thesis. In title on title page [g̳a̳m̳m̳a̳] appear as lower case Greek letters.<br>Includes bibliographical references (pages. 162-178).<br>by Nathaniel Schafheimer.<br>Ph.D.

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Beers, Stephen Andrew. "Studies of the roles of high charge and a lack of tryptophan residues on the properties of human group 11A secreted phospholipase Aâ‚‚." Thesis, University of Southampton, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270393.

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ABABOU, ABDESSAMAD. "Contribution a l'etude des proteines par fluorescence temporelle : etude de l'heterogeneite des declins de fluorescence des proteines a un seul residu tryptophane." Université Louis Pasteur (Strasbourg) (1971-2008), 1998. http://www.theses.fr/1998STR13117.

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L'etude du comportement dynamique des proteines en solution constitue une etape indispensable, si l'on veut comprendre au niveau fondamental les fonctions biologiques multiples de ces edifices moleculaires. La spectroscopie de fluorescence resolue en temps peut apporter differentes informations sur la dynamique interne des proteines en solution. Souvent les proteines a un seul residu tryptophane (trp) presentent des cinetiques de fluorescence heterogenes (plus qu'une composante dans leur declin de fluorescence). Cette heterogeneite a ete largement associee a l'existence des equilibres acide-ba

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Larvor, Marie-Pierre. "Antigenicite, immunogenicite et conformation d'un peptide de 11 residus reconnu par un anticorps monoclonal specifique de la sous-unite beta 2 de la tryptophane synthase d'e. Coli." Paris 7, 1993. http://www.theses.fr/1993PA077067.

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Afin de preciser le mecanisme de l'interaction antigene/anticorps, des etudes ont ete entreprises avec des peptides synthetiques et un anticorps monoclonal dirige contre la sous-unite beta 2 de la tryptophane synthase d'e. Coli. L'un des peptides, long de 11 residus, est reconnu par l'anticorps monoclonal avec une affinite presqu'aussi forte que celle de la proteine native beta 2. Il a ete montre que ce peptide n'est pas immunogenique et qu'il n'existe donc pas obligatoirement de correlation entre l'antigenicite et l'immunogenicite d'un peptide. L'etude du peptide 11 en solution par rmn du pro

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Book chapters on the topic "Tryptophan residue"

1

Chen, Lin X. Q., and Graham R. Fleming. "Photophysics of the Tryptophan Residue in RNaseTl and RNase Tl-2′GMP Complex." In Fluorescent Biomolecules. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5619-6_44.

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Yamakura, Fumiyuki, Takashi Matsumoto, Hikari Taka, Tsutomu Fujimura, and Kimie Murayama. "6-Nitrotryptophan: A Specific Reaction Product Of Tryptophan Residue In Human Cu, Zn-Sod Treated With Peroxynitrite." In Advances in Experimental Medicine and Biology. Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0135-0_88.

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Smith, Bryan John. "Chemical Cleavage of Proteins at Tryptophan Residues." In Springer Protocols Handbooks. Humana Press, 1996. http://dx.doi.org/10.1007/978-1-60327-259-9_64.

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Woolley, G. A., and B. A. Wallace. "Circular dichroism studies of tryptophan residues in gramicidin." In Peptides. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_87.

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Gratton, Enrico, J. Ricardo Alcala, and Gerard Marriott. "Rotational Motions of Tryptophan and Tyrosine Residues in Proteins." In Structure and Dynamics of Nucleic Acids, Proteins, and Membranes. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5308-9_11.

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Léonard, J., E. Portuondo-Campa, A. Cannizzo, et al. "Tryptophan Residues as Natural Ultrafast Voltmeters in Retinal Proteins." In Springer Series in Chemical Physics. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-95946-5_176.

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Takai, K., H. Yoshii, H. Yasui, and Y. Sasai. "THE MECHANISM OF DEHYDROGENATION OF TRYPTOPHAN RESIDUES BY TRYPTOPHAN SIDE-CHAIN OXIDASE II FROM PSEUDOMONAS." In Progress in Tryptophan and Serotonin Research 1986, edited by David A. Bender, Michael H. Joseph, Walter Kochen, and Hans Steinhart. De Gruyter, 1987. http://dx.doi.org/10.1515/9783110854657-017.

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Hansen, J. E., S. J. Rosenthal, and G. R. Fleming. "Subpicosecond Fluorescence Anisotropy Measurements of Tryptophanyl Residues in Proteins." In Springer Series in Chemical Physics. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-84269-6_166.

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Nakamaru, Eiko, Takaaki Kawashima, Yoshiki Kamiyama, Hidefumi Yoshii, Akira Kanda, and Katsuji Takai. "Enzymatic derivatizations of tryptophan residues in peptides and proteins, free tryptophan, and its metabolites with tryptophan side chain oxidase types I and II from Pseudomonas." In Amino Acids. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-011-2262-7_132.

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Toptygin, Dmitri. "Analysis of Time-Dependent Red Shifts in Fluorescence Emission from Tryptophan Residues in Proteins." In Methods in Molecular Biology. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-649-8_9.

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Conference papers on the topic "Tryptophan residue"

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Unno, Masashi, Sadato Kikuchi, Shinji Masuda, P. M. Champion, and L. D. Ziegler. "Structural Refinement of a Key Tryptophan Residue in the BLUF Photoreceptor AppA by Ultraviolet Resonance Raman Spectroscopy." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482713.

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Schlamadinger, Diana E., Hannah S. Shafaat, Katheryn M. Sanchez, et al. "Tryptophan Residues as Membrane Protein Anchors." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482447.

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Eftink, Maurice R. "Transient effects in the solute quenching of tryptophan residues in proteins." In OE/LASE '90, 14-19 Jan., Los Angeles, CA, edited by Joseph R. Lakowicz. SPIE, 1990. http://dx.doi.org/10.1117/12.17705.

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Hasselbacher, Carol A., Elena Rusinova, Evan Waxman, et al. "Probing the structure of human tissue factor by site-directed mutagenesis of tryptophan residues and in-vivo incorporation of tryptophan analogs." In OE/LASE '94, edited by Joseph R. Lakowicz. SPIE, 1994. http://dx.doi.org/10.1117/12.182739.

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Hudson, Bruce S., and Dan Harris. "Mutagenic effects on the fluorescence of tryptophan residues in bacteriophage T4 lysozyme: correlation with dynamics." In OE/LASE '92, edited by Joseph R. Lakowicz. SPIE, 1992. http://dx.doi.org/10.1117/12.58204.

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Pannekok, H., A. J. Van Zonneveid, C. J. M. de vries, M. E. MacDonald, H. Veerman, and F. Blasi. "FUNCTIONAL PROPERTIES OF DELETION-MUTANTS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643724.

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Over the past twenty-five years, genetic methods have generated a wealth of information on the regulation and the structure-function relationship of bacterial genes.These methods are based on the introduction of random mutations in a gene to alter its function. Subsequently, genetic techniques cure applied to localize the mutation, while the nature of the impairedfunction could be determined using biochemical methods. Classic examples of this approach is now considered to be the elucidation of the structure and function of genes, constituting the Escherichia coli lactose (lac) and tryptophan (

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Tauc, Patrick, Luc Fetler, Guy Herve, Moncef Ladjmi, and Jean-Claude Brochon. "Analysis of the role of tryptophan residues in aspartate transcarbamylase by site-directed mutagenesis and fluorescence measurements." In OE/LASE '92, edited by Joseph R. Lakowicz. SPIE, 1992. http://dx.doi.org/10.1117/12.58279.

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Ten, Galina, Natalia Shcherbakova, and Victor Baranov. "Theoretical analysis of environmental influence on the electronic spectra of tryptophanic residues in albumin." In Saratov Fall Meeting 2018: Laser Physics, Photonic Technologies, and Molecular Modeling, edited by Vladimir L. Derbov. SPIE, 2019. http://dx.doi.org/10.1117/12.2523282.

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Casas-Finet, Jose R. "Fluorimetric characterization of tryptophan residues in Escherichia coli single-stranded DNA-binding (SSB) protein and its poly(dT) complex." In OE/LASE '94, edited by Joseph R. Lakowicz. SPIE, 1994. http://dx.doi.org/10.1117/12.182709.

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Reports on the topic "Tryptophan residue"

1

Woolley, G. A., and B. A. Wallace. Circular Dichroism Studies of Tryptophan Residues in Gramicidin. Defense Technical Information Center, 1992. http://dx.doi.org/10.21236/adp008376.

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Schiffer, M., C. H. Chang, and F. J. Stevens. The functions of tryptophan residues in membrane proteins. Office of Scientific and Technical Information (OSTI), 1994. http://dx.doi.org/10.2172/10172497.

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