1,987
Views
11
CrossRef citations to date
0
Altmetric
Review

Genetically modified proteins: functional improvement and chimeragenesis

, , &
Pages 262-274 | Received 26 Jun 2015, Accepted 17 Jul 2015, Published online: 20 Aug 2015

References

  • Stalz H, Roth U, Schleuder D, Macht M, Haebel S, Strupat K, Peter-Katalinic J, Hanisch FG. The Geodia cydonium galectin exhibits prototype and chimera-type characteristics and a unique sequence polymorphism within its carbohydrate recognition domain. Glycobiology 2006; 16:402-14; PMID:16449348
  • Ruan K-H, Cervantes V, So SP. Engineering of a novel hybrid enzyme: an anti-inflammatory drug target with triple catalytic activities directly converting arachidonic acid into the inflammatory prostaglandin E2. Prot Engin Design Select 2009; 22:733-40; http:/dx.doi.org/10.1093/protein/gzp058
  • Bruel L, Sulzenbacher G, Tison MC, Pujol A, Nicoletti C, Perrier J, Galinier A, Ropartz D, Fons M, Pompeo F, et al. α-Galactosidase/sucrose kinase (AgaSK), a novel bifunctional enzyme from the human microbiome coupling galactosidase and kinase activities. J Biol Chem 2011; 286:40814-23; PMID:21931163; http://dx.doi.org/10.1074/jbc.M111.286039
  • Meceron R, Foucault M, Haser R, Mattes R, Watzlawick H, Gouet P. Crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites. J Biol Chem 2012; 28:39642-52; http://dx.doi.org/10.1074/jbc.M112.394114
  • Aydin C, Mukherjee S, Hanson AM, Frick DN, Schiffer CA. The interdomain interface in bifunctional enzyme protein 3/4A (NS3/4A) regulates protease and helicase activities Prot Sci 2013; 22:1786-98; PMID:24123290
  • Kasaragod P, Venkatesan R, Kiema TR, Hiltunen JK, Wierenga RK. Crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites. J Biol Chem 2010; 285:24089-98; PMID:20463028; http://dx.doi.org/10.1074/jbc.M110.117606
  • Jia B, Cheong GW, Zhang S. Multifunctional enzymes in archaea: promiscuity and moonlight. Extremophiles 2013; 17:193-203; PMID:23283522; http://dx.doi.org/10.1007/s00792-012-0509-1
  • Sankhala RS, Lokareddy RK, Cingolani G. Structure of Human PIR1, an Atypical Dual-Specificity Phosphatase. Biochemistry 2014; 53:862-871; PMID:24447265; http://dx.doi.org/10.1021/bi401240x
  • Gu X. Functional divergence in protein (family) sequence evolution. Genetica 2003; 118:133-41; PMID:12868604; http://dx.doi.org/10.1023/A:1024197424306
  • Philippe H, Casane D, Gribaldo S, Lopez P, Meunier J. Heterotachy and functional shift in protein evolution. IUBMB Life 2003; 55:257-65
  • Siltberg-Liberles J, Grahnen JA, Liberles DA. The evolution of protein structures and structural ensembles under functional constraint. Genes (Basel) 2011; 2:748-62; PMID:24710290
  • Harms MJ, Thornton JW. Evolutionary biochemistry: revealing the historical and physical causes of protein properties. Nat Rev Genet 2013; 14:559-71; PMID:23864121; http://dx.doi.org/10.1038/nrg3540
  • Liberles DA, Teichmann SA, Bahar I, Bastolla U, Bloom J, Bornberg-Bauer E, Colwell LJ, de Koning APJ, Dokholyan NV, Echave J, et al. The interface of protein structure, protein biophysics, and molecular evolution. Prot Sci 2012; 21:769-85
  • Lynch M. Evolutionary diversification of the multimeric states of proteins. Proc Natl Acad Sci U S A 2013; 110:E2821-28; PMID:23836639
  • Huang TT, del Valle Marcos ML, Hwang JK, Echave J. A mechanistic stress model of protein evolution accounts for site-specific evolutionary rates and their relationship with packing density and flexibility. BMC Evol Biol 2014; 14:78; PMID:24716445; http://dx.doi.org/10.1186/1471-2148-14-78
  • Marcos ML, Echave J. Too packed to change: side-chain packing and site-specific substitution rates in protein evolution. PeerJ 2015; 3:e911; PMID:25922797
  • Schulenburg C, Hilvert D. Protein conformational disorder and enzyme catalysis. Top Curr Chem 2013; 337:41-67; PMID:23536241; http://dx.doi.org/10.1007/128_2012_411
  • van der Lee R, Buljan M, Lang B, Weatheritt RJ, Daughdrill GW, Dunker AK, Fuxreiter M, Gough J, Gsponer J, Jones DT. Classification of intrinsically disordered regions and proteins. Chem Rev 2014; 114:6589-631; PMID:24773235; http://dx.doi.org/10.1021/cr400525m
  • Liu Z, Huang Y. Advantages of proteins being disordered. Prot Sci 2014; 23:539-50; http://dx.doi.org/10.1002/pro.2443
  • Warnecke T, Weber CC, Hurst LD. Why there is more to protein evolution than protein function: splicing, nucleosomes and dual-coding sequence. Biochem Soc Trans 2009; 37:756-61; PMID:19614589; http://dx.doi.org/10.1042/BST0370756
  • Nishida H, Kondo S, Nojiri H, Noma K, Oshima K. Evolutionary mechanisms of microbial genomes. Int J Evol Biol 2011; 2011:319479; PMID:21716727
  • Chaparro-Riggers JF, Polizzi KM, Bommarius AS. Better library design: data-driven protein engineering. Biotechnol J 2007; 2:180-191; PMID:17183506; http://dx.doi.org/10.1002/biot.200600170
  • Basit N, Wechsler H. Prediction of enzyme mutant activity using computational mutagenesis and incremental transduction. Adv Bioinformatics 2011; 2011:958129; PMID:22007208; http://dx.doi.org/10.1155/2011/958129
  • Vyas VK, Ukawala RD, Ghate M, Chintha C. Homology modeling a fast tool for drug discovery: current perspectives. Indian J Pharm Sci 2012; 74:1-17; PMID:23204616; http://dx.doi.org/10.4103/0250-474X.102537
  • Taylor WR, Hamilton RS, Sadowski MI. Prediction of contacts from correlated sequence substitutions. Curr Opin Struct Biol 2013; 23:473-79; PMID:23680395; http://dx.doi.org/10.1016/j.sbi.2013.04.001
  • Pronk S, Páll S, Schulz R, Larsson P, Bjelkmar P, Apostolov R, Shirts MR, Smith JC, Kasson PM, van der Spoel D, et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 2013; 29:845-54; PMID:23407358; http://dx.doi.org/10.1093/bioinformatics/btt055
  • Rose PW, Prli A, Bi C, Bluhm WF, Christie CH, Dutta S, Green RK, Goodsell DS, Westbrook JD, Woo J, et al. The RCSB Protein Data Bank: views of structural biology for basic and applied research and education. Nuc Acids Res 2014; 43:D345-56; http://dx.doi.org/10.1093/nar/gku1214
  • Baker M. Protein engineering: navigating between chance and reason. Nat methods 2011; 8:623-26; PMID:21799494; http://dx.doi.org/10.1038/nmeth.1654
  • Koga N, Tatsumi-Koga R, Liu G, Xiao R, Acton TB, Montelione GT, Baker D. Principles for designing ideal protein structures. Nature 2012; 8: 491(7423):222-7; PMID:23135467; http://dx.doi.org/10.1038/nature11600
  • Zhang WH, Otting G, Jackson CJ. Protein engineering with unnatural amino acids. Curr Opin Struct Biol 2013; 23:581-87; PMID:23835227; http://dx.doi.org/10.1016/j.sbi.2013.06.009
  • Yadahalli S, Hemanth VV, Rao G, Gosavi S. Modeling non-native interactions in designed proteins. Isr J Chem 2014; 54:1230-40; http://dx.doi.org/10.1002/ijch.201400035
  • Matthaei JF, DiMaio F, Richards JJ, Pozzo LD, Baker D, Baneyx F. Designing two-dimensional protein arrays through fusion of multimers and computational interface redesign. Nano Lett 2015; PMID:25986921
  • Dimitrov DS. Therapeutic proteins. Methods Mol Biol 2012; 899:1-26
  • Wang P. Nanoscale engineering for smart biocatalysts with fine-tuned properties and functionalities. Top Catal 2012; 55(16-18):1107-13; PMID:22752519
  • Kruger B, Liang C, Prell F, Fieselmann A, Moya A, Schuster S, Volker U, Dandekar T. Metabolic adaptation and protein complexes in prokaryotes. Metabolites 2012; 2:940-58; PMID:24957769; http://dx.doi.org/10.3390/metabo2040940
  • Carrera J, Estrela R, Luo J, Rai N, Tsoukalas A, Tagkopoulos I. An integrative, multi-scale, genome-wide model reveals the phenotypic landscape of Escherichia coli. Mol Syst Biol 2014; 10:735; PMID:24987114; http://dx.doi.org/10.15252/msb.20145108
  • Winkler U, Saftel W, Stabenau H. A new type of a multifunctional - oxidation enzyme in Euglena. Plant Physiol 2003; 131:753-62; PMID:12586899; http://dx.doi.org/10.1104/pp.013151
  • Nam H, Lewis NE, Lerman JA, Lee DH, Chang RL, Kim D, Palsson BO. Network context and selection in the evolution to enzyme specificity. Science 2012; 337:1101-04; PMID:22936779
  • Kohrer C, RajBhandary UL. Protein Engineering. Nucleic Acids and Molecular Biology, edited by Gross HJ, 2009. Springer-Verlag Berlin Heidelberg
  • Turanli-Yildiz B, Alkim C, Cakar ZP. Protein Engineering Methods and Applications. Protein Engineering, edited by Kaumaya P, 2012. InTech, http://www.intechopen.com/books/protein-engineering/protein-engineering-methods-and-applications
  • Meunier B. Hybrid molecules with a dual mode of action: dream or reality? Acc Chem Res 2008; 41:69-77; PMID:17665872; http://dx.doi.org/10.1021/ar7000843
  • Palmer AE, Qin Y, Park JG, McCombs JE. Design and application of genetically encoded biosensors. Trends Biotechnol 2011; 29:144-52; PMID:21251723; http://dx.doi.org/10.1016/j.tibtech.2010.12.004
  • Kim SB, Izumi H. Functional artificial luciferases as an optical readout for bioassays Sung Bae Kim, Hiroshi Izumi. Biochem Biophys Res Comm 2014; 448:418-23; PMID:24802399; http://dx.doi.org/10.1016/j.bbrc.2014.04.128
  • Balabanova L, Golotin V, Kovalchuk S, Bulgakov A, Likhatskaya G, Son O, Rasskazov V. A novel bifunctional hybrid with marine bacterium alkaline phosphatase and Far Eastern holothurian mannan-binding lectin activities. PLoS One 2014; 9(11):e112729; http://dx.doi.org/10.1371/journal.pone.0112729
  • McLachlan MJ, Sullivan RP, Zhao H. Directed enzyme evolution and high-throughput screening. Biocatalysis for the pharmaceutical industry: discovery, development, and manufacturing, edited by Tao J, Lin GQ, Liese A, 2009. John Wiley & Sons Asia (Pte) Ltd
  • Amin SR, Erdin S, Ward RM, Lua RC, Lichtarge O. Prediction and experimental validation of enzyme substrate specificity in protein structures. Proc Natl Acad Sci U S A 2013; 110:E4195-202; PMID:24145433; http://dx.doi.org/10.1073/pnas.1305162110
  • Golotin V, Balabanova L, Likhatskaya G, Rasskazov V. Recombinant production and characterization of a highly active alkaline phosphatase from marine bacterium Cobetia marina. Mar Biotechnol 2015; 17:130-43
  • Takehiro N, Takeshi S, Tomoaki M, Tetsuya Y. Directed evolution of proteins through in vitro protein synthesis in liposomes. J Nucleic Acids 2012; 2012:923214; http://dx.doi.org/10.1155/2012/923214; PMID:22957209
  • Yong KJ, Scott DJ. Rapid directed evolution of stabilized proteins with cellular high-throughput encapsulation solubilization and screening (CHESS). Biotechnol Bioeng 2015; 112:438-46; PMID:25220691; http://dx.doi.org/10.1002/bit.25451
  • Raymond A, Lovell S, Lorimer D, Walchli J, Mixon M, Wallace E, Thompkins K, Archer K, Burgin A, Stewart L. Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer. BMC Biotechnol 2009; 9:37; PMID:19383143; http://dx.doi.org/10.1186/1472-6750-9-37
  • Makino T, Skretas G, Georgiou G. Strain engineering for improved expression of recombinant proteins in bacteria. Microb Cell Fact 2011; 10:32.; PMID:21569582; http://dx.doi.org/10.1186/1475-2859-10-32
  • Schaepe S, Levisauskas D, Simutis R, Lübbert A. Data-based optimization of protein production processes. Biotechnol Lett 2014; 36:929-35; PMID:24557076; http://dx.doi.org/10.1007/s10529-013-1448-3
  • Gomes S, Leonor IB, Mano JF, Reis RL, Kaplan DL. Natural and genetically engineered proteins for tissue engineering. Prog Polym Sci 2012; 37:1-17; PMID:22058578; http://dx.doi.org/10.1016/j.progpolymsci.2011.07.003
  • Parrilli E, Papa R, Tutino ML, Sannia G, Engineering of a psychrophilic bacterium for the bioremediation of aromatic compounds. Bioeng Bugs 2010; 1:213-16
  • Mukherjee AK, Rai SK, Bordoloi NK. Biodegradation of waste chicken-feathers by an alkaline b-keratinase (Mukartinase) purified from a mutant Brevibacillus sp. strain AS-S10-II. Int Biodeterior Biodegradation 2011; 65:1229-37; http://dx.doi.org/10.1016/j.ibiod.2011.09.007
  • Al-Zahrani NHM. Improving ability of Pseudomonas putida strain to biosynthesis of L-tryptophan. Life Sci J 2014; 11:476-81
  • Sadhu S, Ghosh PK, Aditya G, Maiti TK. Optimization and strain improvement by mutation for enhanced cellulase production by Bacillus sp. (MTCC10046) isolated from cow dung. J King Saud Univ Sci 2014; 26:323-32; http://dx.doi.org/10.1016/j.jksus.2014.06.001
  • Blagodatski A, Katanaev VL. Technologies of directed protein evolution in vivo. Cell Mol Life Sci 2011; 68:1207-14; PMID:21190058; http://dx.doi.org/10.1007/s00018-010-0610-5
  • Çelik E, Çalık P. Production of recombinant proteins by yeast cells. Biotechnol Adv 2012; 30(5):1108-18
  • Nielsen J. Production of biopharmaceutical proteins by yeast. Bioengineered 2013; 4:207-11
  • Gopal GJ, Kumar A. Strategies for the production of recombinant protein in Escherichia coli. Protein J 2013; 32:419-25; PMID:23897421; http://dx.doi.org/10.1007/s10930-013-9502-5
  • Weinstock MT, Jacobsen MT, Kay MS. Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity. Proc Natl Acad Sci U S A 2014; 111:11679-84; PMID:25071217; http://dx.doi.org/10.1073/pnas.1410900111
  • Jakob F, Lehmann C, Martinez R, Schwaneberg V. Increasing protein production by directed vector backbone evolution. AMB Express 2013; 3:39; PMID:23890095; http://dx.doi.org/10.1186/2191-0855-3-39
  • Rahman RNZRA, Zakaria II, Salleh AB, Basri M. Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens. Int J Mol Sci 2012; 13:9673-91; PMID:22949824; http://dx.doi.org/10.3390/ijms13089673
  • Lisurek M, Simgen B, Antes I, Bernhardt R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. ChemBioChem 2008; 9:1439-49; PMID:18481342; http://dx.doi.org/10.1002/cbic.200700670
  • Spadiut O, Pisanelli I, Maischberger T, Peterbauer C, Gorton L, Chaiyen P, Haltrich D. Engineering of pyranose 2-oxidase: improvement for biofuel cell and food applications through semi-rational protein design. J Biotechnol 2009; 139:250-57; PMID:19095017; http://dx.doi.org/10.1016/j.jbiotec.2008.11.004
  • Umekawa M, Li C, Higashiyama T, Huang W, Ashida H, Yamamoto K, Wang L-X. Efficient glycosynthase mutant derived from Mucor hiemalis endo-β-N- acetylglucosaminidase capable of transferring oligosaccharide from both sugar Oxazoline and natural N-glycan. J Biol Chem 2010; 285:511-21; PMID:19880511; http://dx.doi.org/10.1074/jbc.M109.059832
  • Hediger MR, De Vico L, Rannes JB, Jäckel C, Besenmatter W, Svendsen A, Jensen JH. In silico screening of 393 mutants facilitates enzyme engineering of amidase activity in CalB. PeerJ 2013; 1:e145
  • Han R, Liu L, Shin H-D, Chen RR, Li J, Du G, Chend J. Systems engineering of tyrosine 195, tyrosine 260, and glutamine 265 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance maltodextrin specificity for 2-O-D-glucopyranosyl-L-ascorbic acid synthesis. App Environ Microbiol 2013; 79:672-77; http://dx.doi.org/10.1128/AEM.02883-12
  • Dong Q, Wang J, Yang H, Wei C, Yu J, Zhang Y, Huang Y, Zhang XE, Wei H. Construction of a chimeric lysin Ply187N-V12C with extended lytic activity against staphylococci and streptococci. Microb Biotechnol 2014; 8:210-20; PMID:25219798
  • Johnston CA, Whitney DS, Volkman BF, Doe CQ, Prehoda KE. Conversion of the enzyme guanylate kinase into a mitotic-spindle orienting protein by a single mutation that inhibits GMP-induced closing. Proc Natl Acad Sci U S A 2011; 108:E973-8; PMID:21990344; http://dx.doi.org/10.1073/pnas.1104365108
  • Glenn WS, Nims E, O'Connor SE. Reengineering a tryptophan halogenase to preferentially chlorinate a direct alkaloid precursor. J Am Chem Soc 2011; 133:19346-9; PMID:22050348; http://dx.doi.org/10.1021/ja2089348
  • Nishioka T, Yasutake Y, Nishiya Y, Tamura T. Structure-guided mutagenesis for the improvement of substrate specificity of Bacillus megaterium glucose1-dehydrogenase IV. FEBS J 2012; 279:3264-75; PMID:22804868; http://dx.doi.org/10.1111/j.1742-4658.2012.08713.x
  • Gao X, Cui W, Ning Ding, Zhongmei Liu, Yaping Tian, Zhemin Zhou. Structure-based approach to alter the substrate specificity of Bacillus subtilis aminopeptidase. Prion 2013; 7:328-34
  • Webster CI, Burrell M, Olsson L-L, Fowler SB, Digby S, Sandercock A, Snijder A, Tebbe J, Haupts U, Grudzinska J, et al. Engineering neprilysin activity and specificity to create a novel therapeutic for Alzheimer's disease. PLoS One 2014; 9:e104001
  • Ishida T. Effects of point mutation on enzymatic activity: correlation between protein electronic structure and motion in chorismate mutase reaction. J Am Chem Soc 2010; 132:7104-18; PMID:20426479; http://dx.doi.org/10.1021/ja100744h
  • Currin A, Swainston N, Day PJ, Kell DB. Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently. Chem Soc Rev 2015; 44:1172-239; PMID:25503938; http://dx.doi.org/10.1039/C4CS00351A
  • de Melo FHM, Butera D, Medeiros RS, Andrade LNS, Nonogaki S, Soares FA, Alvarez RA, da Silva AMM, Chammas R. Biological applications of a chimeric probe for the assessment of galectin-3 ligands. J Histochem Cytochem 2007; 55:1015-26; PMID:17565118; http://dx.doi.org/10.1369/jhc.7A7174.2007
  • Michelow SC, Dong M, Mungall BA, Yantosca LM, Lear C, Ji X, Karpel M, Rootes CL, Brudner M, Houen G, et al. A novel L-ficolin/mannose-binding lectin chimeric molecule with enhanced activity against Ebola virus. J Biol Chem 2010; 285:24729-39; PMID:20516066; http://dx.doi.org/10.1074/jbc.M110.106260
  • Grebenik EA, Generalova AN, Nechaev AV, Khaydukov EV, Mironova KE, Stremovskiy OA, Lebedenko EN, Zvyagin AV, Deyev SM. Specific visualization of tumor cells using upconversion nanophosphors. Acta Naturae 2014; 6:48-53; PMID:25558394
  • Richter A, Eggenstein E, Skerra A. Anticalins: Exploiting a non-Ig scaffold with hypervariable loops for the engineering of binding proteins. FEBS Lett 2014; 588:213-18; PMID:24239535; http://dx.doi.org/10.1016/j.febslet.2013.11.006
  • Reddy VA, Venu K, Rao DE, Rao KV, Reddy VD. Chimeric gene construct coding for bi-functional enzyme endowed with endoglucanase and phytase activities. Arch Microbiol 2009; 191:171-5; PMID:18987844; http://dx.doi.org/10.1007/s00203-008-0437-8
  • Furtado GP, Ribeiro LF, Lourenzoni MR, Ward RJ. A designed bifunctional laccase/b-1,3–1,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse. Protein Eng Des Sel 2013; 26:15-23; PMID:23012443
  • Rizk M, Elleuche S, Antranikian G. Generating bifunctional fusion enzymes composed of heat-active endoglucanase (Cel5A) and endoxylanase (XylT). Biotechnol Lett 2015; 37:139-45; PMID:25214221; http://dx.doi.org/10.1007/s10529-014-1654-7
  • Otsuka R, Imai S, Murata T, Nomura Y, Okamoto M, Tsumori H, Kakuta E, Hanada N, Momoi Y. Application of chimeric glucanase comprising mutanase and dextranase for prevention of dental biofilm formation. Microbiol Immunol 2015; 59:28-36; PMID:25411090; http://dx.doi.org/10.1111/1348-0421.12214
  • Reddy Chichili VP, Kumar V, Sivaraman J. Linkers in the structural biology of protein–protein interactions. Prot Sci 2013; 22:153-67
  • Deyev SM, Lebedenko EN. Modern technologies for creating synthetic antibodies for clinical application. Acta naturae 2009; 1:32-50; PMID:22649585
  • Cannon JP, O'Driscoll M, Litman GW. Construction, expression, and purification of chimeric protein reagents based on immunoglobulin fc regions. Methods Mol Biol 2011; 48:51-67; http://dx.doi.org/10.1007/978-1-61779-139-0_4
  • Banta S, Dooley K, Shur O. Replacing antibodies: engineering new binding proteins. Annu Rev Biomed Eng 2013; 15:93-113; PMID:23642248; http://dx.doi.org/10.1146/annurev-bioeng-071812-152412
  • Alewine C, Hassan R, Pastan I. Advances in anticancer immunotoxin therapy. The Oncologist 2015; 20:176-85; PMID:25561510; http://dx.doi.org/10.1634/theoncologist.2014-0358
  • Li T, Huang S, Jiang WZ, Wright D, Spalding MH, Weeks DP, Yang B. TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain. Nuc Acids Res 2011; 39:359-72
  • Gheybi E, Amani J, Salmanian AH, Mashayekhi F, Khodi S. Designing a recombinant chimeric construct contain MUC1 and HER2 extracellular domain for prediagnostic breast cancer. Tumour Biol 2014; 35:11489-97; PMID:25128064; http://dx.doi.org/10.1007/s13277-014-2483-y
  • Ruan X, Sack DA, Zhang W. Genetic fusions of a CFA/I/II/IV MEFA (Multiepitope Fusion Antigen) and a toxoid fusion of heat-stable toxin (STa) and heat-labile toxin (LT) of enterotoxigenic Escherichia coli (ETEC) retain broad anti-CFA and antitoxin antigenicity. PLoS One 2015; 10(3):e0121623
  • Ugwu SO, Apte SP. The effect of buffers on protein conformational stability. Pharmaceutical Technology 2004; 86-113
  • Zarrine-Afsar A, Zhang Z, Schweiker KL, Makhatadze GI, Davidson AR, Chan HS. Kinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain proteins. Adv Exp Med Biol 2012; 80:858-70
  • Griffin MD, Gerrard JA. The relationship between oligomeric state and protein function. Adv Exp Med Biol 2012; 747:74-90; PMID:22949112; http://dx.doi.org/10.1007/978-1-4614-3229-6_5
  • Karan R, Capes MD, Sarma SD. Function and biotechnology of extremophilic enzymes in low water activity. Aquat Biosyst 2012, 8:4
  • Struvay C, Feller G. Optimization to low temperature activity in psychrophilic enzymes. Int J Mol Sci 2012; 13:11643-65; PMID:23109875; http://dx.doi.org/10.3390/ijms130911643
  • Morelli A, Haugner J, Seelig B. Thermostable artificial enzyme isolated by in vitro selection. PLoS One 2014; 9(11):e112028; http://dx.doi.org/10.1371/journal.pone.0113256
  • Yu H, Huang H. Engineering proteins for thermostability through rigidifying flexible sites. Biotechnol Adv 2014; 32:308-15; PMID:24211474; http://dx.doi.org/10.1016/j.biotechadv.2013.10.012

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.