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| | C. Robert Matthews, PhD - BMP Faculty - UMass Medical School |
 | | Gloss L.M., Matthews C.R. Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. | | | Gloss, L.M., Matthews C.R. Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. | | | Steinbach, P.J., Ionescu, R., Matthews, C.R. Analysis of Kinetics Using a Hybrid Maximum-Entropy/Nonlinear-Least-Squares Method: Application to Protein Folding. |
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http://www.umassmed.edu/bmp/faculty/matthews.cfm?start=Publications
(797 words)
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| | bioc0007.doc |
| | - calorimetry biosensors clinical chemistry molecular biology/genetic engineering techniques in clinical biochemistry Content (Protein Biochemistry): - Protein stabilisation, denaturation, folding mechanisms, ligand interaction. | | | Content (Analytical Biochemistry): Modern analytical techniques and approaches currently being used and developed within the various fields of biochemistry. | | | - discuss the factors determining protein stabilisation, denaturation, folding mechanisms and ligand interaction. |
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http://www.gre.ac.uk/schools/cls/bioc0007.doc
(269 words)
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| | CSUF Chemistry: K. P. Wong |
| | McCoy, L.F. and Wong, K.P. "The Denaturation of Bovine Erythrocyte Carbonic Anhydrase B Denatured by Acid, Heat, and Detergent," Biochemistry 20, 3062-3067 (1981). | | | Wong, K.P. and Hamlin, L.M. "The Acid Denaturation of Carbonic Anhydrase," Biochemistry 13, 2678 (1974). | | | McCoy, L.F. and Wong, K.P. "The Denaturation and Renaturation of Cobalt Carbonic Anhydrase B from Bovine Erythrocyte," Biopolymers 18, 2893-2904 (1979). |
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http://www.csufresno.edu/Chemistry/welcome/facultydir/kpwong.html
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| | C. Nick Pace |
| | Pace, C.N., Laurents, D.V., and Erickson, R.E. (1992) "Urea Denaturation of Barnase: pH Dependence and Characterization of the Unfolded State." Biochemistry, 31, 2728-2734. | | | Hu, C.Q., Sturtevant, J.M., Thomson, J.A., Erickson, R.E., and Pace, C.N. (1992) "Thermodynamics of Ribonuclease T1 Denaturation." Biochemistry, 31, 4876-4882. | | | Myers, J.K., Pace, C.N., and Scholtz, J.M. (1997) "Helix Propensities Are Identical in Proteins and Peptides." Biochemistry, 36, 10923-10929. |
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http://pauling.tamu.edu/medbiogen/faculty/cnp.html
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| | Dr. Faizan Ahmad, Department of Biosciences |
| | If high concentrations of urea, which by themselves are enough to induce denaturation, are added to the salt-induced denaturation, the product of denaturation is in the urea-denatured-state. | | | Syed Ehtaishamul Haque, "Thermodynamic Studies of Denaturation of Cytochrome-C by Urea and Guanidine Hydrochloride". | | | Characterization of molten globule states of proteins (BBA, 2003; Biochemistry, 2003). |
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http://jmi.nic.in/Fnat/faizan_bio.htm
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| | JCE 1999 (76) 1283 [Sep] Determination of Myoglobin Stability by Visible Spectroscopy |
| | The denaturation of myoglobin by the chaotropic salt guanidium hydrochloride is readily and reproducibly followed at 409 nm, and the free energy of stabilization of the native protein is derived from a straightforward mathematical analysis of the denaturation profile. | | | A simple system for the determination of protein stability by denaturation is described. | | | Biochemistry; Proteins/ Peptides; Biophysical Chemistry; Laboratory Instruction |
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http://jchemed.chem.wisc.edu/journal/Issues/1999/Sep/abs1283.html
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| | Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology. |
| | Ogawa, R. Miyagi, T. Tamiya, T. Tsuchiya, Comparison of the stability of fish light meromyosins by guanidine hydrochloride denaturation, Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology 122 (4) (1999) pp. | | | Takenaka, J. Inagaki, S. Tsuyama, K. Miyatake, Y. Nakano, Cell cycle dependent ADP-ribosylation of a unicellular organism, Euglena gracilis Z, Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology 111B (2) (1995) pp. |
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http://www.elsevier.com/cdweb/journals/03050491/viewer.htt?viewtype=authors&rangeselected=194
(247 words)
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| | Denaturation (biochemistry) - Wikipedia, the free encyclopedia |
| | In biochemistry, denaturation is a structural change in biomolecules such as nucleic acids and proteins, such that they are no longer in their native state (the shape which allows for optimal biological activity). | | | The denaturation of nucleic acids such as DNA, also called melting, is the separation of a double strand into two single strands, which occurs when the hydrogen bonds between the strands are broken. | | | In quaternary structure denaturation, protein sub-units are dissociated and/or the spatial arrangement of protein subunits is disrupted. |
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http://en.wikipedia.org/wiki/Denaturation_(biochemistry)
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| | Denaturation - Wikipedia, the free encyclopedia |
| | denaturation (biochemistry), in biochemistry, a structural change in macromolecules caused by extreme conditions. | | | Denaturation (fissile materials) of fissile materials, the process of transforming them so that they cannot be used in nuclear weapons. | | | Denatured alcohol, the intentional adulteration of ethyl alcohol so that it is unsuitable as a beverage. |
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http://en.wikipedia.org/wiki/Denaturation
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| | Paul D. Boyer Quotes |
| | But solving how oxidative phosphorylation occurred remained one the most challenging problems of biochemistry, and I could not resist its siren call. | | | Her death contributed to my later interest in studying biochemistry, an interest that has not been fulfilled in the sense that my accomplishments remain more at the basic than the applied level. | | | This led to the discovery that long chain fatty acids would remarkably stabilize serum albumin to heat denaturation, and would even reverse the denaturation by heat or concentrated urea solutions. |
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http://www.brainyquote.com/quotes/authors/p/paul_d_boyer.html
(1015 words)
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| | Denaturation (biochemistry) - Wikipedia, the free encyclopedia |
| | In biochemistry, denaturation is a structural change in biomolecules such as nucleic acids and proteins, such that they are no longer in their native state, and their shape which allows for optimal activity. | | | The denaturation of nucleic acids such as DNA due to high temperatures, is the separation of a double strand into two single strands, which occurs when the hydrogen bonds between the strands are broken. | | | In quaternary structure denaturation, protein sub-units are dissociated and/or the spatial arrangement of protein subunits is disrupted. |
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http://en.wikipedia.org/wiki/Denaturation_(Biochemistry)
(705 words)
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| | OldPapers |
| | Hermans J, Rialdi G: Heat of ionization and denaturation of sperm whale myoglobin determined with a microcalorimeter. | | | Jerusalem Symposia on Quantum Chemistry and Biochemistry, 1981, Reidel, Dordrecht, Holland, 331-342. | | | Knoll DA, Hermans J: Effect of poly(ethylene glycol) on protein denaturation and model compound pKa. |
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http://hekto.med.unc.edu:8080/HERMANS/OldPapers
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| | Denaturation - Wikipedia, the free encyclopedia |
| | Denaturation, in biochemistry, is a structural change in macromolecules caused by extreme conditions. | | | Denaturation of fissile materials is the process of transforming them so that they cannot be used in nuclear weapons. | | | Denaturation can refer to the intentional adulteration of ethyl alcohol so that it is unsuitable as a beverage. |
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http://en.wikipedia.org/wiki/Denaturation
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| | Celia Schiffer, Ph.D. - Faculty - Biochemistry and Molecular Pharmacology - UMass Medical School |
| | Schiffer, C.A., Dötsch, V., Wüthrich, K., van Gunsteren, W.F, "Exploring the Role of the Solvent in the Denaturation of a Protein: A Molecular Dynamics Study of the DNA Binding Domain of the 434 Repressor." Biochemistry Vol. | | | Schiffer, C.A., Clifton, I.J., Davisson, V.J., Santi, D.V., Stroud, R.M. "The Crystal Structure of Human Thymidylate Synthase: A Structural Mechanism for Guiding Substrates into the Active Site." Biochemistry Vol. | | | Schiffer, C.A., Huber,R., Wüthrich, K., van Gunsteren, W.F., "Simultaneous Refinement of the Structure of BPTI against NMR data measured in solution and X-ray data measured in single crystals." J. |
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http://www.umassmed.edu/pharmacology/faculty/schiffer.cfm?start=0
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| | NMR-Detected Order in Core Residues of Denatured Bovine Pancreatic Trypsin Inhibitor |
| | Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701, Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, and Department of Biochemistry, University of Minnesota, St. | | | Varying concentrations of urea are required to completely unfold different protein segments, indicating that global denaturation is not two-state. | | | With increasing urea concentration, a denatured conformation, D, is populated and contributes to the intensity of the u-peak, since for a given NH a chemical shift difference between P |
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http://pubs.acs.org/cgi-bin/jtextd?bichaw/40/32/html/bi010483z.html
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| | Publications - John Philo |
| | C., Zheng, M., Hutchins, R., and Philo, J. The inorganic biochemistry of photosynthetic water oxidation. | | | Narhi, L. O., Philo, J. S., Sun, B., Chang, B. S., and Arakawa, T. Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor. | | | Narhi, L. O., Philo, J. S., Li, T. S., Zhang, M., Samal, B., and Arakawa, T. Induction of a-helix in the b-sheet protein tumor necrosis factor-a: Thermal- and trifluoroethanol-induced denaturation at neutral pH. |
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http://www.ap-lab.com/philo_bibliography.htm
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| | IUB Chemistry REU - Projects |
| | Cold denaturation is well known for proteins but has never before been observed in nucleic acid biochemistry. | | | We are also looking into the potential biological roles of cold denaturation in conjunction with a non-coding RNA, DsrA, that acts as a translational regulator of genes involved in the cold shock, a pre-programmed set of physiological changes that respond to reduced environmental temperature. | | | The state of the art for enzymatically active nucleic acids is to define the range of reactions that ribozymes can catalyze, the mechanisms by which they function, and their capacity to participate in biology. |
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http://chemlearn.chem.indiana.edu/reu/biochemistry.htm
(609 words)
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| | Wilfredo Colón |
| | Hobart, S. A., Meinhold, D., Osuna R., and Colón W. From Two-State to Three-State: Effect of P61A Mutation on the Dynamics and Stability of the Factor for Inversion Stimulation Results in an Altered Equilibrium Denaturation Mechanism (2002) Biochemistry, 41, 13744-13754. | | | Understanding how the amino acid sequence of a protein determines its three-dimensional structure remains one of the greatest unsolved problems in biochemistry. | | | One hypothesis is that kinetic intermediates play an important role in protein folding by directing the process along a productive pathway, and by reducing the number of conformations that a protein needs to search through to reach the native structure. |
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http://www.rpi.edu/dept/chem/yesterday/faculty/colon/colon.html
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| | Biochemistry |
| | Biochemistry: is the study of the chemical composition and reactions of living matter. | | | Denaturation is incompatible with the biologic function of the protein because it causes rearrangement of the protein& active site. | | | Most forms of denaturation are reversible, however if the temperature change or Ph change is too sever the protein may be irreversibly denatured, that is, damaged beyond repair. |
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http://www.etsu.edu/cpah/hsci/forsman/Biochemistry.htm
(2886 words)
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| | Encyclopedia: Protein |
| | Cheese In biochemistry, denaturation is a structural change in biomolecules such as nucleic acids and proteins, such that they are no longer in their native state (the shape which allows for optimal biological activity). | | | An electrolyte is a substance which dissociates free ions when dissolved (or molten), to produce an electrically conductive medium. | | | The title of this article begins with a capital letter, due to technical limitations of the MediaWiki software. |
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http://www.nationmaster.com/encyclopedia/Protein
(6044 words)
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| | Amazon.com: Biocalorimetry: Applications of Calorimetry in the Biological Sciences: Books: John E. Ladbury,Babur Z. Chowdhry,John E. Ladbury,Babur Z. Chowdhry |
| | Biocalorimetry: Applications of Calorimetry in the Biological Sciences is the first book to bring together an overview of the two key methods in calorimetry, (isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC)), with a wide variety of biological applications, such as DNA-drug/protein interactions, protein-protein (ligand) interactions and protein denaturation studies. | | | This book will be of interest to researchers working in biochemistry, biophysics and molecular biology, particularly those in the pharmaceutical, food and biotechnology industries. | | | In addition, Biocalorimetry: Applications of Calorimetry in the Biological Sciences provides valuable insight for lecturers and students, (particularly final year undergraduates and postgraduates), for teaching purposes, as well as for understanding the theoretical basis and wider practical applications of calorimetry. |
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http://www.amazon.com/exec/obidos/tg/detail/-/0471977810?v=glance
(563 words)
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| | Group Publications |
| | Bennion, B.J. and V. Daggett, Counteraction of urea-induced protein denaturation by trimethylamine N-oxide: A chemical chaperone at atomic resolution, Proceedings of the National Academy of Sciences USA, 101, 6433-6438, 2004. | | | Bennion, B.J., DeMarco, M. and V. Daggett, Preventing misfolding of the prion protein by Trimethylamine N-oxide, Biochemistry, 4 1, 12955-12963, 2004. |
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http://www.staff.washington.edu/~daglab/vd_publications.htm
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| | Staphylococcus aureus Expresses a Major Histocompatibility Complex Class II Analog -- Jönsson et al. 270 (37): 21457 -- Journal of Biological Chemistry |
| | From the (1)Center for Extracellular Matrix Biology and Department of Biochemistry and Biophysics, Institute of Biosciences and Technology, Texas A and M University, Houston, Texas 77030-3303 and the (2)University of Mannitoba, Winnipeg, Manitoba R3E OW2, Canada | | | The reaction mixtures were overlaid with 100 µl of mineral oil and amplified for 30 cycles consisting of a 1-min denaturation period at 94 °C, a 1-min anneal temperature at 55 °C, and a 1-min extension period at 72 °C. After amplification, 10 µl was analyzed by agarose gel electrophoresis (1% agarose). | | | To whom correspondence and reprint requests should be addressed: Institute of Biosciences and Technology, 2121 West Holcombe Blvd., Houston, TX Tel.: 713-677-7551; Fax: 713-677-7576; mhook{at}ibt.tamu.edu. |
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http://www.jbc.org/cgi/content/full/270/37/21457
(563 words)
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| | Ada E. Yonath, LIST OF PUBLICATIONS |
| | · A. Yonath, A. Podjarny, B. Honig, W. Traub, A. Sielecki, O. Herzberg and J. Moult, Structural analysis of denaturant-protein interactions: comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme, Biophys Struct Mech, 4, 27-36 (1977) | | | Sodium dodecyl sulfate induced structural changes in triclinic lysozyme, Biochemistry, 16, 1418-24 (1977) | | | · *A. Sielecki and A.Yonath, Conformational adjustment to substrate binding in crystals of triclinic lysozyme, In: "Biomolecular Structure, Conformation, Function and Evolution" (R. Srinivasan Ed) Pergamon Press, Oxford, NY, 1, 201-4 (1980) |
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http://www.weizmann.ac.il/sb/faculty_pages/Yonath/00Publications.html
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