Journal articles on the topic 'Isothermal denaturation'
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Hinrichs, Jörg, and Britta Rademacher. "High pressure thermal denaturation kinetics of whey proteins." Journal of Dairy Research 71, no. 4 (2004): 480–88. http://dx.doi.org/10.1017/s0022029904000238.
Full textSarver, Ronald W., Joseph M. Rogers, and Dennis E. Epps. "Determination of Ligand-MurB Interactions by Isothermal Denaturation: Applicatio as a Secondary Assay to Complement High Throughput Screening." Journal of Biomolecular Screening 7, no. 1 (2002): 21–28. http://dx.doi.org/10.1177/108705710200700104.
Full textNIELSEN, Anders D., Claus C. FUGLSANG, and Peter WESTH. "Effect of calcium ions on the irreversible denaturation of a recombinant Bacillus halmapalus alpha-amylase: a calorimetric investigation." Biochemical Journal 373, no. 2 (2003): 337–43. http://dx.doi.org/10.1042/bj20030220.
Full textCLAEYS, WENDIE L., ANN M. VAN LOEY та MARC E. HENDRICKX. "Kinetics of alkaline phosphatase and lactoperoxidase inactivation, and of β-lactoglobulin denaturation in milk with different fat content". Journal of Dairy Research 69, № 4 (2002): 541–53. http://dx.doi.org/10.1017/s0022029902005721.
Full textIstrate, Daniel, Crisan Popescu та Martin Möller. "Non-Isothermal Kinetics of Hardα-Keratin Thermal Denaturation". Macromolecular Bioscience 9, № 8 (2009): 805–12. http://dx.doi.org/10.1002/mabi.200800344.
Full textShi, Chao, Fanjin Shang, Meiling Zhou, Pansong Zhang, Yifan Wang, and Cuiping Ma. "Triggered isothermal PCR by denaturation bubble-mediated strand exchange amplification." Chemical Communications 52, no. 77 (2016): 11551–54. http://dx.doi.org/10.1039/c6cc05906f.
Full textHuang, Mengting, Fang Yang, Jiye Fu, Pengfeng Xiao, Jing Tu, and Zuhong Lu. "Reaction parameter comparison and optimization of multiple displacement amplification." Analytical Methods 12, no. 1 (2020): 46–53. http://dx.doi.org/10.1039/c9ay01922g.
Full textWafer, Lucas, Marek Kloczewiak, Sharon M. Polleck, and Yin Luo. "Isothermal chemical denaturation of large proteins: Path-dependence and irreversibility." Analytical Biochemistry 539 (December 2017): 60–69. http://dx.doi.org/10.1016/j.ab.2017.10.001.
Full textEpps, Dennis E., Ronald W. Sarver, Joseph M. Rogers, John T. Herberg, and Paul K. Tomich. "The Ligand Affinity of Proteins Measured by Isothermal Denaturation Kinetics." Analytical Biochemistry 292, no. 1 (2001): 40–50. http://dx.doi.org/10.1006/abio.2001.5047.
Full textMaltzeva, Yulia I., Daria A. Gorbenko, Ekaterina V. Nikitina, Maria S. Rubel, and Dmitry M. Kolpashchikov. "Visual Detection of Stem-Loop Primer Amplification (SPA) Products without Denaturation Using Peroxidase-like DNA Machines (PxDM)." International Journal of Molecular Sciences 24, no. 9 (2023): 7812. http://dx.doi.org/10.3390/ijms24097812.
Full textAugustijn, Dillen, Alina Kulakova, Sujata Mahapatra, Pernille Harris, and Åsmund Rinnan. "Isothermal Chemical Denaturation: Data Analysis, Error Detection, and Correction by PARAFAC2." Analytical Chemistry 92, no. 10 (2020): 6958–67. http://dx.doi.org/10.1021/acs.analchem.9b05748.
Full textOWUSU-APENTEN, RICHARD K. "REVISED CONFORMATIONAL STABILITY PARAMETERS FOR BETA-LACTOGLOBULIN ISOTHERMAL DENATURATION BY UREA." Journal of Food Biochemistry 26, no. 3 (2002): 181–90. http://dx.doi.org/10.1111/j.1745-4514.2002.tb00851.x.
Full textSchön, Arne, Benjamin R. Clarkson, Maria Jaime, and Ernesto Freire. "Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry." Proteins: Structure, Function, and Bioinformatics 85, no. 11 (2017): 2009–16. http://dx.doi.org/10.1002/prot.25354.
Full textCHEN, FUR-CHI, Y. H. PEGGY HSIEH, ROGER C. BRIDGMAN, and AGNES KILONZO-NTHENGE. "Kinetics of Tropomyosin Denaturation as a Predictive Model for Verifying Thermal Processing of Beef Products." Journal of Food Protection 69, no. 10 (2006): 2447–53. http://dx.doi.org/10.4315/0362-028x-69.10.2447.
Full textChen, S. S., N. T. Wright, and J. D. Humphrey. "Heat-Induced Changes in the Mechanics of a Collagenous Tissue: Isothermal, Isotonic Shrinkage." Journal of Biomechanical Engineering 120, no. 3 (1998): 382–88. http://dx.doi.org/10.1115/1.2798005.
Full textMahran, R., N. Vello, A. Komulainen, H. Härmä, and K. Kopra. "64P Isothermal chemical KRAS denaturation assay for monitoring stability and inhibitors interactions." ESMO Open 8, no. 1 (2023): 100922. http://dx.doi.org/10.1016/j.esmoop.2023.100922.
Full textChandran, Harish, Nikhil Gopalkrishnan, Bernard Yurke, and John Reif. "Meta-DNA: synthetic biology via DNA nanostructures and hybridization reactions." Journal of The Royal Society Interface 9, no. 72 (2012): 1637–53. http://dx.doi.org/10.1098/rsif.2011.0819.
Full textFRANCO, Ricardo, Guangyue BAI, Vesna PROSINECKI, Filipa ABRUNHOSA, Gloria C. FERREIRA, and Margarida BASTOS. "Porphyrin-substrate binding to murine ferrochelatase: effect on the thermal stability of the enzyme." Biochemical Journal 386, no. 3 (2005): 599–605. http://dx.doi.org/10.1042/bj20040921.
Full textBEHBAHANI, G. REZAEI, M. SHALBAFAN, N. GHEIBI, et al. "DENATURATION OF HUMAN SERUM ALBUMIN BY CERIUM (III) CHLORIDE." Biophysical Reviews and Letters 08, no. 01n02 (2013): 59–71. http://dx.doi.org/10.1142/s1793048013500033.
Full textHartdégen, Márton, András József Laki, Kolos Farkasvölgyi, Kristóf Iván, and Judit Plutzer. "Evaluation of Touchdown Loop-Mediated Isothermal Amplification for the Detection of Giardia duodenalis." Parasitologia 5, no. 2 (2025): 25. https://doi.org/10.3390/parasitologia5020025.
Full textNasreen, Khalida, Zahoor Ahmad Parray, Shahzaib Ahamad, et al. "Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders." Biomolecules 10, no. 3 (2020): 490. http://dx.doi.org/10.3390/biom10030490.
Full textSuzuki, Ryota, Masaru Ihira, Yoshihiko Enomoto, et al. "Heat denaturation increases the sensitivity of the cytomegalovirus loop-mediated isothermal amplification method." Microbiology and Immunology 54, no. 8 (2010): 466–70. http://dx.doi.org/10.1111/j.1348-0421.2010.00236.x.
Full textSenisterra, Guillermo A., Bum Soo Hong, Hee-Won Park, and Masoud Vedadi. "Application of High-Throughput Isothermal Denaturation to Assess Protein Stability and Screen for Ligands." Journal of Biomolecular Screening 13, no. 5 (2008): 337–42. http://dx.doi.org/10.1177/1087057108317825.
Full textShahrajabian, Mohamad H., Wenli Sun, and Qi Cheng. "Different Methods for Molecular and Rapid Detection of Human Novel Coronavirus." Current Pharmaceutical Design 27, no. 25 (2021): 2893–903. http://dx.doi.org/10.2174/1381612827666210604114411.
Full textBAJAJ, Kanika, Ghadiyaram CHAKSHUSMATHI, Kiran BACHHAWAT-SIKDER, Avadhesha SUROLIA, and Raghavan VARADARAJAN. "Thermodynamic characterization of monomeric and dimeric forms of CcdB (controller of cell division or death B protein)." Biochemical Journal 380, no. 2 (2004): 409–17. http://dx.doi.org/10.1042/bj20031528.
Full textTaneja, S., and F. Ahmad. "Increased thermal stability of proteins in the presence of amino acids." Biochemical Journal 303, no. 1 (1994): 147–53. http://dx.doi.org/10.1042/bj3030147.
Full textChen, S. S., N. T. Wright, and J. D. Humphrey. "Heat-Induced Changes in the Mechanics of a Collagenous Tissue: Isothermal Free Shrinkage." Journal of Biomechanical Engineering 119, no. 4 (1997): 372–78. http://dx.doi.org/10.1115/1.2798281.
Full textRoss, Patrick, Wilhelm Weihofen, Fai Siu, et al. "Isothermal chemical denaturation to determine binding affinity of small molecules to G-protein coupled receptors." Analytical Biochemistry 473 (March 2015): 41–45. http://dx.doi.org/10.1016/j.ab.2014.11.019.
Full textSoroka, Marianna, Barbara Wasowicz, and Anna Rymaszewska. "Loop-Mediated Isothermal Amplification (LAMP): The Better Sibling of PCR?" Cells 10, no. 8 (2021): 1931. http://dx.doi.org/10.3390/cells10081931.
Full textCLAEYS, WENDIE L., LINDA R. LUDIKHUYZE, ANN M. VAN LOEY та MARC E. HENDRICKX. "Inactivation kinetics of alkaline phosphatase and lactoperoxidase, and denaturation kinetics of β-lactoglobulin in raw milk under isothermal and dynamic temperature conditions". Journal of Dairy Research 68, № 1 (2001): 95–107. http://dx.doi.org/10.1017/s002202990000460x.
Full textDatta, Nivedita, Maurice G. Hayes, Hilton C. Deeth, and Alan L. Kelly. "Significance of frictional heating for effects of high pressure homogenisation on milk." Journal of Dairy Research 72, no. 4 (2005): 393–99. http://dx.doi.org/10.1017/s0022029905001056.
Full textTang, Chuanning, Scott Lew, and Dacheng He. "Using a second-order differential model to fit data without baselines in protein isothermal chemical denaturation." Protein Science 25, no. 4 (2016): 898–904. http://dx.doi.org/10.1002/pro.2878.
Full textHarris, J. L., P. B. Wells, and J. D. Humphrey. "Altered Mechanical Behavior of Epicardium Due to Isothermal Heating Under Biaxial Isotonic Loads." Journal of Biomechanical Engineering 125, no. 3 (2003): 381–88. http://dx.doi.org/10.1115/1.1567754.
Full textSaboury, A. A., M. Miroliae, M. Nemat-Gorgani, and A. A. Moosavi-Movahedi. "Kinetics denaturation of yeast alcohol dehydrogenase and the effect of temperature and trehalose. An isothermal microcalorimetry study." Thermochimica Acta 326, no. 1-2 (1999): 127–31. http://dx.doi.org/10.1016/s0040-6031(98)00588-7.
Full textSarver, Ronald W., Joseph M. Rogers, and Dennis E. Epps. "Determination of Ligand-MurB Interactions by Isothermal Denaturation: Application as a Secondary Assay to Complement High Throughput Screening." Journal of Biomolecular Screening 7, no. 1 (2002): 21–28. http://dx.doi.org/10.1089/108705702753520305.
Full textRubio, Ana R., Natalia Busto, José M. Leal, and Begoña García. "Doxorubicin binds to duplex RNA with higher affinity than ctDNA and favours the isothermal denaturation of triplex RNA." RSC Advances 6, no. 103 (2016): 101142–52. http://dx.doi.org/10.1039/c6ra21387a.
Full textHaque, M. Amdadul, Peter Aldred, Jie Chen, Colin J. Barrow, and Benu Adhikari. "Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes." Food Chemistry 141, no. 2 (2013): 702–11. http://dx.doi.org/10.1016/j.foodchem.2013.03.035.
Full textGooran, Negin, and Kari Kopra. "Fluorescence-Based Protein Stability Monitoring—A Review." International Journal of Molecular Sciences 25, no. 3 (2024): 1764. http://dx.doi.org/10.3390/ijms25031764.
Full textLiu, Mengmeng, Mengzhe Li, Cuiping Ma, and Chao Shi. "Detection of canine parvovirus and feline panleukopenia virus in fecal samples by strand exchange amplification." Journal of Veterinary Diagnostic Investigation 32, no. 6 (2020): 880–86. http://dx.doi.org/10.1177/1040638720962067.
Full textFleischman, Marianna L., Rajoshi Chaudhuri, Ria T. Caringal, Lisa Kueltzo, K. C. Cheng, and Frank Arnold. "Optimization of Formulation Conditions for Broadly Neutralizing Antibodies (bnAb): Utilizing Isothermal Chemical Denaturation as a High-throughput Screening Method." Biophysical Journal 116, no. 3 (2019): 334a. http://dx.doi.org/10.1016/j.bpj.2018.11.1817.
Full textKushwah, Vinita Chauhan, Ritika Chauhan, and Ram Kumar Dhaked. "Fluorescence Thermal Shift Assay based High Through-put Screening in Small Molecule Drug Discovery: A Brief Overview." Journal of Modern Biology and Drug Discovery 3 (May 28, 2024): 3. http://dx.doi.org/10.53964/jmbdd.2024003.
Full textNye, Dillon B., and Nathan A. Tanner. "Chimeric DNA byproducts in strand displacement amplification using the T7 replisome." PLOS ONE 17, no. 9 (2022): e0273979. http://dx.doi.org/10.1371/journal.pone.0273979.
Full textLicheri, Matthias, Manon Flore Licheri, Kemal Mehinagic, Nicolas Ruggli, and Ronald Dijkman. "A Novel and Rapid Selective Viral Genome Amplification and Sequencing Method for African Swine Fever Virus." Viruses 16, no. 11 (2024): 1664. http://dx.doi.org/10.3390/v16111664.
Full textNai, Yi Heng, Egan H. Doeven, and Rosanne M. Guijt. "An improved nucleic acid sequence-based amplification method mediated by T4 gene 32 protein." PLOS ONE 17, no. 3 (2022): e0265391. http://dx.doi.org/10.1371/journal.pone.0265391.
Full textLiu, Wentao, and Guoying Li. "Non-isothermal kinetic analysis of the thermal denaturation of type I collagen in solution using isoconversional and multivariate non-linear regression methods." Polymer Degradation and Stability 95, no. 12 (2010): 2233–40. http://dx.doi.org/10.1016/j.polymdegradstab.2010.09.012.
Full textSvilenov, Hristo, Uroš Markoja, and Gerhard Winter. "Isothermal chemical denaturation as a complementary tool to overcome limitations of thermal differential scanning fluorimetry in predicting physical stability of protein formulations." European Journal of Pharmaceutics and Biopharmaceutics 125 (April 2018): 106–13. http://dx.doi.org/10.1016/j.ejpb.2018.01.004.
Full textCotrina, Ellen Y., Ângela Oliveira, José Pedro Leite, et al. "Repurposing Benzbromarone for Familial Amyloid Polyneuropathy: A New Transthyretin Tetramer Stabilizer." International Journal of Molecular Sciences 21, no. 19 (2020): 7166. http://dx.doi.org/10.3390/ijms21197166.
Full textJensen, Jaime L., Beau D. Jernberg, Sangita C. Sinha, and Christopher L. Colbert. "Structural basis of cell-surface signaling by a conserved sigma regulator in Gram-negative bacteria." Journal of Biological Chemistry 295, no. 17 (2020): 5795–806. http://dx.doi.org/10.1074/jbc.ra119.010697.
Full textSultana, Tajnin, David M. Morgan, Beau D. Jernberg, Peyton Zak, Sangita C. Sinha, and Christopher L. Colbert. "Biophysical and Solution Structure Analysis of Critical Residues Involved in the Interaction between the PupB N-Terminal Signaling Domain and PupR C-Terminal Cell Surface Signaling Domain from Pseudomonas capeferrum." Biomolecules 14, no. 9 (2024): 1108. http://dx.doi.org/10.3390/biom14091108.
Full textTrollope, K. M., J. F. Görgens та H. Volschenk. "Semirational Directed Evolution of Loop Regions in Aspergillus japonicus β-Fructofuranosidase for Improved Fructooligosaccharide Production". Applied and Environmental Microbiology 81, № 20 (2015): 7319–29. http://dx.doi.org/10.1128/aem.02134-15.
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