Kumar S, Tsai CJ, Nussinov R. Factors enhancing protein thermostability. Protein Eng. 2000;13(3):179-91. [
Link] [
DOI:10.1093/protein/13.3.179]
Talluri S. Advances in engineering of proteins for thermal stability. Int J Adv Biotechnol Res. 2011;2(1):190-200. [
Link]
Gill P, Tohidi Moghadam T, Ranjbar B. Differential scanning calorimetry techniques: Applications in biology and nanoscience. J Biomol Tech. 2010; 21(4):167-93. [
Link]
Graziano G, Catanzano F, Giancola C, Barone G. DSC Study of the thermal stability of S-protein and S-peptide/S-protein complexes. Biochemistry. 1996;35(41):13386-92. [
Link] [
DOI:10.1021/bi960856+]
Protasevich I, Ranjbar B, Lobachov V, Makarov A, Gilli R, Briand C, et al. Conformation and thermal denaturation of apocalmodulin: Role of electrostatic mutations. Biochemistry. 1997;36(8)2017-24. [
Link] [
DOI:10.1021/bi962538g]
Tsuji FI, Ohmiya Y, Fagan TF, Toh H, Inouye S. Molecular evolution of the Ca2+-binding photoproteins of the Hydrozoa. Photochem Photobiol. 1995;62(4):657-61. [
Link] [
DOI:10.1111/j.1751-1097.1995.tb08713.x]
Aghamaali MR1, Jafarian V, Sariri R, Molakarimi M, Rasti B, Taghdir M, et al. Cloning, sequencing, expression and structural investigation of mnemiopsin from Mnemiopsis leidyi: An attempt toward understanding ca2+-regulated photoproteins. Protein J. 2011;30(8):566-74. [
Link] [
DOI:10.1007/s10930-011-9363-8]
Moncrief ND, Kretsinger RH, Goodman M. Evolution of EF-hand calcium-modulated proteins: I. relationships based on amino acid sequences. J Mol Evol. 1990;30(6):522-62. [
Link] [
DOI:10.1007/BF02101108]
Gonzalez JE, Tsien RY. Improved indicators of cell membrane potential that use fluorescence resonance energy transfer. Chem Biol. 1997;4(4):269-77. [
Link] [
DOI:10.1016/S1074-5521(97)90070-3]
Blinks JR. Use of photoproteins as intracellular calcium indicators. Environ Health Perspect. 1990;84:75-81. [
Link] [
DOI:10.1289/ehp.908475]
Lewis CJ, Daunert S. Photoproteins as luminescent labels in binding assays. Fresenius J Anal Chem. 2000;366(6-7):760-8. [
Link] [
DOI:10.1007/s002160051570]
Stepanyuk GA, Liu ZJ, Burakova LP, Lee J, Rose J, Vysotski ES, et al. Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state. Biochim Biophys Acta. 2013;1834(10)2139-46. [
Link] [
DOI:10.1016/j.bbapap.2013.07.006]
Ward WW, Seliger HH. Properties of mnemiopsin and berovin, calcium-activated photoproteins from the Ctenophores Mnemiopsis species and Beroe ovata. Biochemistry. 1974;13(7):1500-10. [
Link] [
DOI:10.1021/bi00704a028]
Ward WW, Seliger HH. Extraction and purification of calcium-activated photoproteins from the ctenophores Mnemiopsis species and Beroe ovata. Biochemistry. 1974;13(7):1491-9. [
Link] [
DOI:10.1021/bi00704a027]
Takenaka Y, Yamaguchi A, Tsuruoka N, Torimura M, Gojobori T, Shigeri Y. Evolution of bioluminescence in marine planktonic copepods. Mol Biol Evol. 2006;29(6):1669-81. [
Link] [
DOI:10.1093/molbev/mss009]
Liu ZJ, Stepanyuk GA, Vysotski ES, Lee J, Markova SV, Malikova NP, et al. Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state. Proc Natl Acad Sci USA. 2006;103(8);2570-5. [
Link] [
DOI:10.1073/pnas.0511142103]
Deng L, Vysotski ES, Markova SV, Liu ZJ, Lee J, Rose, et al. All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obeli. Protein Sci. 2005;14(2):663-75. [
Link] [
DOI:10.1110/ps.041142905]
Head JF, Inouye S, Teranishi K, Shimomura O. The crystal structure of the photoprotein aequorin at 2.3 A resolution. Nature. 2000;405(6784):372-76. [
Link] [
DOI:10.1038/35012659]
Dikici E, Qu X, Rowe L, Millner L, Logue C, Deo SK, et al. Aequorin variants with improved bioluminescence properties. Protein Eng Des Sel. 2009;22(4):243-8. [
Link] [
DOI:10.1093/protein/gzn083]
Mahdavi A, Sajedi RH, Hosseinkhani S, Taghdir M, Sariri R. Site-directed mutagenesis of photoprotein mnemiopsin: Implication of some conserved residues in bioluminescence properties. Photochem Photobiol Sci. 2013;12(3):467-78. [
Link] [
DOI:10.1039/C2PP25320H]
Jafarian V, Sariri R, Hosseinkhani S, Aghamaali MR, Sajedi RH, Taghdir M, et al. A unique EF-hand motif in mnemiopsin photoprotein from Mnemiopsis leidyi: Implication for its low calcium sensitivity. Biochem Biophys Res Commun. 2011;413(2):164-70. [
Link] [
DOI:10.1016/j.bbrc.2011.08.022]
Mahdavi A, Sajedi RH, Hosseinkhani S, Taghdir M. Hyperactive Arg39Lys mutated mnemiopsin: Implication of positively charged residue in chromophore binding cavity. Photochem Photobiol Sci. 2015;14(4):792-800. [
Link] [
DOI:10.1039/C4PP00191E]
Ranjbar B, Gill P. Circular dichroism techniques: Biomolecular and nanostructural analyses- a review. Chem Biol Drug Des. 2009;74(2):101-20. [
Link] [
DOI:10.1111/j.1747-0285.2009.00847.x]
Wang W, Malcolm BA. Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange Site-Directed Mutagenesis. Biotechniques. 1999;26(4):680-2. [
Link] [
DOI:10.2144/99264st03]
Chen YH, Yang JT, Martinez HM. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry. 1972;11(22):4120-31. [
Link] [
DOI:10.1021/bi00772a015]
Maghami P, Ranjbar B, Hosseinkhani S, Ghasemi A, Moradi A, Gill P. Relationship between stability and bioluminescence color of firefly luciferase. Photochem Photobiol Sci. 2010;9(3):376-83. [
Link] [
DOI:10.1039/b9pp00161a]
Hakiminia F, Rnjbar B, Khalifeh Kh, Khajeh Kh. Kinetic and thermodynamic properties of Pseudomonas fluorescence lipase upon addition of proline. Int J Biolo Macromol. 2013;55:123-6. [
Link] [
DOI:10.1016/j.ijbiomac.2012.12.046]
Freire E, Biltonen RL. Statistical mechanical deconvolution of thermal transitions in macromolecules. I. Theory and application to homogeneous systems. biopolymers. 1978;17(2):463-79. [
Link] [
DOI:10.1002/bip.1978.360170212]
Protein Structure Modeling With MODELLER. Current protocols in bioinformatics. John Wiley& Sons Inc; 2006. 15:5.6.1-5.6.30. [
Link]
Smith CA, Kortemme T. Backrub-like Backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction. J Mol Biol. 2008;380(4):742-56. [
Link] [
DOI:10.1016/j.jmb.2008.05.023]
Tina KG, Bhadra R, Srinivasan N. PIC: Protein interactions calculator. Nucleic Acids Res. 2007;35:473-6. [
Link] [
DOI:10.1093/nar/gkm423]
Willard L, Ranjan A, Zhang H, Monzavi H, Boyko RF, Sykes BD, et al. VADAR: A web server for quantitative evaluation of protein structure quality. Nucleic Acids Res. 2003;31(13):3316-9. [
Link] [
DOI:10.1093/nar/gkg565]
Bornot A, Etchebest C, De Brevern AG. Predicting protein flexibility through the prediction of local structures. Proteins. 2011;79(3):839-52. [
Link] [
DOI:10.1002/prot.22922]
De Brevern AG, Bornot A, Craveur P, Etchebest C, Gelly JC. PredyFlexy: flexibility and local structure prediction from sequenc. 2012;40: 317-22. [
Link]
Serdyuk IN, Zaccai NR, Zaccai J. Methods in molecular biophysics: Structure, dynamics, function. Cambridge: Cambridge University Press; 2007. [
Link] [
DOI:10.1017/CBO9780511811166]
Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 157(1):105-32. [
Link] [
DOI:10.1016/0022-2836(82)90515-0]
