Abstract
Coiled-coil is a well characterized secondary structure in proteins. It was first described in 1953 by Crick as the main structural element of a large class of fibrous proteins (included keratin, myosin, and fibrinogen) based on the X-ray diffraction pattern of α-keratin [1, 2]. The first identification of the primary sequence of coiled-coil containing protein tropomyosin in 1972 [3] and the first high-resolution crystal structure characterization of a three stranded coiled-coil hemagglutinin and two stranded (CAP) in 1981 [4] gave scientists great inspiration and courage to further prove that the coiled-coil structure is the key dimerization element in a class of transcriptional factors—the Leucine Zipper proteins [5]. Since then, hundreds of coiled-coil structures were identified and even the high-resolution crystal structures were obtained.
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Appendices
Appendix 4.1 List of the Synthetic Peptides and Their Molecular Weights
Name | Peptide sequence | Calculated | Found |
|---|---|---|---|
CCK-1 | fl-GGGK XAALKEK VAALKEK VAALKE | 2828.3 | 2827.8 |
CCK-2 | fl-GGGK VAAXKEK VAALKEK VAALKE | 2814.3 | 2813.4 |
CCK-3 | fl-GGK VAALKEK XAALKEK VAALKE | 2771.3 | 2770.8 |
CCK-4 | fl-GGK VAALKEK VAAXKEK VAALKE | 2757.3 | 2756.3 |
CCK-5 | fl-GGGK VAALKEK XAALKEK VAALKEK VAALKE | 3567.8 | 3567.1 |
CCK-6 | fl-GGGK VAALKEK VAAXKEK VAALKEK VAALKE | 3553.7 | 3553.0 |
CCK-7 | fl-GGK VAALKEK VAALKEK XAALKEK VAALKE | 3510.7 | 3509.9 |
CCK-8 | fl-GGK VAALKEK VAALKEK VAAXKEK VAALKE | 3496.7 | 3495.9 |
CCE-1 | tmr-GGGE CAALEKE VAALEKE VAALEK | 2825.8 | 2824.7 |
CCE-1′ | tmr-KSEESYECAALEKEVAALEKEVAALEK | 3379.1 | 3377.8 |
CCE-2 | tmr-GGGE VAACEKE VAALEKE VAALEK | 2811.9 | 2810.7 |
CCE-3 | tmr-GGE VAALEKE CAALEKE VAALEK | 2768.8 | 2767.2 |
CCE-4 | tmr-GGE VAALEKE VAACEKE VAALEK | 2755.8 | 2754.3 |
CCE-5 | tmr-GGGE VAALEKE CAALEKE VAALEKE VAALEK | 3566.3 | 3566.0 |
CCE-6 | tmr-GGGE VAALEKE VAACEKE VAALEKE VAALEK | 3552.3 | 3551.9 |
CCE-7 | tmr-GGE VAALEKE VAALEKE CAALEKE VAALEK | 3509.3 | 3509.1 |
CCE-8 | tmr-GGE VAALEKE VAALEKE VAACEKE VAALEK | 3495.3 | 3494.9 |
tmr-GG XKEKVAALKEKNAALKEKVAALKE | 3239.8 | 3237.9 | |
tmr-KSEESYCEKEVAALEKENAALEKEVAALEK | 3750.3 | 3750.0 | |
P1x | tmr-GG-EXAALKQENQALEQKIAALKGYK | 3131.6 | 3130.5 |
P2c | tmr-GG-ECAALKQKNKYLKQEIQQLE | 2930.0 | 2929.5 |
P3x | fl-GGKXQALQQKIKQLKQKIAALKGY | 3059.4 | 3058.7 |
P4c | fl-GGQCAALEQEIAALEQEIAALE | 2613.4 | 2635.2 (+Na+) |
P5c | Cy5-GG-ECAALEQQNKYLKQEIAALKGK | 3226.7 | 3226.7 |
P6x | Cy5-GG-KXKALKQENAYLQQEIQALK | 3157.2 | 3156.6 |
tmr-GGG KXAALKEKVAALKEKVAALKE | 2882.6 | 2881.8 | |
CCK-1′-dimer | (tmr-GGKXAALKEKIAALKEKIAALKEGG)2KGG | 6160.4 | 6192.7 (+Na+) |
Appendix 4.2 Plasmid Information of pET28m-EGFP-CCE-1
ATG CATCACCATCATCATCATATGGCTAGCATGACTGGTGGACAGCAAATGGGTCGC GGA TCC ATGCATCACCATCATCATCATATGGCTAGCATGACTGGTGGACAGCAAATGGGTCGC GGATCCATGGTGAGCAAGGGCGAGGAGCTGTTCACCGGGGTGGTGCCCATCCTGGTCGAG CTGGACGGCGACGTAAACGGCCACAAGTTCAGCGTGTCCGGCGAGGGCGAGGGCGATGCC ACCTACGGCAAGCTGACCCTGAAGTTCATCTGCACCACCGGCAAGCTGCCCGTGCCCTGG CCCACCCTCGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGCCGCTACCCCGACCAC ATGAAGCAGCACGACTTCTTCAAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCACC ATCTTCTTCAAGGACGACGGCAACTACAAGACCCGCGCCGAGGTGAAGTTCGAGGGCGAC ACCCTGGTGAACCGCATCGAGCTGAAGGGCATCGACTTCAAGGAGGACGGCAACATCCTG GGGCACAAGCTGGAGTACAACTACAACAGCCACAACGTCTATATCATGGCCGACAAGCAG AAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACAACATCGAGGACGGCAGCGTGCAG CTCGCCGACCACTACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCTGCTGCCCGAC AACCACTACCTGAGCACCCAGTCCGCCCTGAGCAAAGACCCCAACGAGAAGCGCGATCAC ATGGTCCTGCTGGAGTTCGTGACCGCCGCCGGGATCACTCTCGGCATGGACGAGCTGTAC AAGGAGCTCAAATCTGAAGAGTCTTATGAATGTGCTGCCTTAGAGAAGGAAGTTGCAGCG TTAGAGAAGGAAGTTGCTGCATTAGAGAAGTAGAAGCTT
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Wang, J. (2016). Coiled-Coil Binding-Induced Covalent Cross-Linking. In: Study of the Peptide-Peptide and Peptide-Protein Interactions and Their Applications in Cell Imaging and Nanoparticle Surface Modification. Springer Theses. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-53399-4_4
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DOI: https://doi.org/10.1007/978-3-662-53399-4_4
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