메뉴 건너뛰기




Volumn 289, Issue 37, 2014, Pages 25460-25467

Harnessing the unique structural properties of isolated α-helices

Author keywords

[No Author keywords available]

Indexed keywords

CELL ENGINEERING; MECHANICAL PROPERTIES; PEPTIDES;

EID: 84907164371     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R114.583906     Document Type: Review
Times cited : (52)

References (44)
  • 2
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structures and assemblies
    • Woolfson, D. N. (2005) The design of coiled-coil structures and assemblies. Adv. Protein Chem. 70, 79-112
    • (2005) Adv. Protein Chem , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 3
    • 84866550686 scopus 로고    scopus 로고
    • Structural attributes for the recognition of weak and anomalous regions in coiled-coils of myosins and other motor proteins
    • Sunitha, M. S., Nair, A. G., Charya, A., Jadhav, K., Mukhopadhyay, S., and Sowdhamini, R. (2012) Structural attributes for the recognition of weak and anomalous regions in coiled-coils of myosins and other motor proteins. BMC Res. Notes 5, 530
    • (2012) BMC Res. Notes , vol.5 , pp. 530
    • Sunitha, M.S.1    Nair, A.G.2    Charya, A.3    Jadhav, K.4    Mukhopadhyay, S.5    Sowdhamini, R.6
  • 4
    • 84883030214 scopus 로고    scopus 로고
    • Coiled-coil response to mechanical force: Global stability and local cracking
    • Kreuzer, S. M., and Elber, R. (2013) Coiled-coil response to mechanical force: global stability and local cracking. Biophys. J. 105, 951-961
    • (2013) Biophys. J , vol.105 , pp. 951-961
    • Kreuzer, S.M.1    Elber, R.2
  • 6
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee, S., Robbins, V. H., and Baldwin, R. L. (1989) Unusually stable helix formation in short alanine-based peptides. Proc. Natl. Acad. Sci. U.S.A. 86, 5286-5290
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 7
    • 0023461350 scopus 로고
    • Helix stabilization by Glu- ...Lys+ salt bridges in short peptides of de novo design
    • Marqusee, S., and Baldwin, R. L. (1987) Helix stabilization by Glu- ...Lys+ salt bridges in short peptides of de novo design. Proc. Natl. Acad. Sci. U.S.A. 84, 8898-8902
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8898-8902
    • Marqusee, S.1    Baldwin, R.L.2
  • 8
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A
    • Bierzynski, A., Kim, P. S., and Baldwin, R. L. (1982) A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proc. Natl. Acad. Sci. U.S.A. 79, 2470-2474
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 2470-2474
    • Bierzynski, A.1    Kim, P.S.2    Baldwin, R.L.3
  • 9
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, B. H., and Bragg, J. K. (1959) Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31, 526-535
    • (1959) J. Chem. Phys , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2
  • 10
    • 0027475153 scopus 로고
    • Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings
    • Huyghues-Despointes, B. M., Scholtz, J. M., and Baldwin, R. L. (1993) Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings. Protein Sci. 2, 80-85
    • (1993) Protein Sci , vol.2 , pp. 80-85
    • Huyghues-Despointes, B.M.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 11
    • 0029020484 scopus 로고
    • N- and C-capping preferences for all 20 amino acids in α-helical peptides
    • Doig, A. J., and Baldwin, R. L. (1995) N- and C-capping preferences for all 20 amino acids in α-helical peptides. Protein Sci. 4, 1325-1336
    • (1995) Protein Sci , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 12
    • 0034788744 scopus 로고    scopus 로고
    • Design of the linkers which effectively separate domains of a bifunctional fusion protein
    • Arai, R., Ueda, H., Kitayama, A., Kamiya, N., and Nagamune, T. (2001) Design of the linkers which effectively separate domains of a bifunctional fusion protein. Protein Eng. 14, 529-532
    • (2001) Protein Eng , vol.14 , pp. 529-532
    • Arai, R.1    Ueda, H.2    Kitayama, A.3    Kamiya, N.4    Nagamune, T.5
  • 13
    • 10344263901 scopus 로고    scopus 로고
    • Conformations of variably linked chimeric proteins evaluated by synchrotron X-ray small-angle scattering
    • Arai, R., Wriggers, W., Nishikawa, Y., Nagamune, T., and Fujisawa, T. (2004) Conformations of variably linked chimeric proteins evaluated by synchrotron X-ray small-angle scattering. Proteins 57, 829-838
    • (2004) Proteins , vol.57 , pp. 829-838
    • Arai, R.1    Wriggers, W.2    Nishikawa, Y.3    Nagamune, T.4    Fujisawa, T.5
  • 14
    • 60049093597 scopus 로고    scopus 로고
    • Insertion of the designed helical linker led to increased expression of Tf-based fusion proteins
    • Amet, N., Lee, H. F., and Shen, W. C. (2009) Insertion of the designed helical linker led to increased expression of Tf-based fusion proteins. Pharm. Res. 26, 523-528
    • (2009) Pharm. Res , vol.26 , pp. 523-528
    • Amet, N.1    Lee, H.F.2    Shen, W.C.3
  • 15
    • 33750583939 scopus 로고    scopus 로고
    • Improving the oral efficacy of recombinant granulocyte colony-stimulating factor and transferrin fusion protein by spacer optimization
    • Bai, Y., and Shen, W. C. (2006) Improving the oral efficacy of recombinant granulocyte colony-stimulating factor and transferrin fusion protein by spacer optimization. Pharm. Res. 23, 2116-2121
    • (2006) Pharm. Res , vol.23 , pp. 2116-2121
    • Bai, Y.1    Shen, W.C.2
  • 16
    • 72049105108 scopus 로고    scopus 로고
    • Protein purification involving a unique auto-cleavage feature of a repeated EAAAK peptide
    • Wu, Y. J., Fan, C. Y., and Li, Y. K. (2009) Protein purification involving a unique auto-cleavage feature of a repeated EAAAK peptide. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 877, 4015-4021
    • (2009) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.877 , pp. 4015-4021
    • Wu, Y.J.1    Fan, C.Y.2    Li, Y.K.3
  • 17
    • 0026565486 scopus 로고
    • Energetic contribution of solvent-exposed ion pairs to α-helix structure
    • Lyu, P. C., Gans, P. J., and Kallenbach, N. R. (1992) Energetic contribution of solvent-exposed ion pairs to α-helix structure. J. Mol. Biol. 223, 343-350
    • (1992) J. Mol. Biol , vol.223 , pp. 343-350
    • Lyu, P.C.1    Gans, P.J.2    Kallenbach, N.R.3
  • 18
  • 19
    • 0035427308 scopus 로고    scopus 로고
    • Cooperative helix stabilization by complex Arg-Glu salt bridges
    • Olson, C. A., Spek, E. J., Shi, Z., Vologodskii, A., and Kallenbach, N. R. (2001) Cooperative helix stabilization by complex Arg-Glu salt bridges. Proteins 44, 123-132
    • (2001) Proteins , vol.44 , pp. 123-132
    • Olson, C.A.1    Spek, E.J.2    Shi, Z.3    Vologodskii, A.4    Kallenbach, N.R.5
  • 20
    • 75149128079 scopus 로고    scopus 로고
    • Myosin VI: An innovative motor that challenged the swinging lever arm hypothesis
    • Spudich, J. A., and Sivaramakrishnan, S. (2010) Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis. Nat. Rev. Mol. Cell Biol. 11, 128-137
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 128-137
    • Spudich, J.A.1    Sivaramakrishnan, S.2
  • 21
    • 0024340027 scopus 로고
    • Cloning and expression of a smooth muscle caldesmon
    • Bryan, J., Imai, M., Lee, R., Moore, P., Cook, R. G., and Lin, W. G. (1989) Cloning and expression of a smooth muscle caldesmon. J. Biol. Chem. 264, 13873-13879
    • (1989) J. Biol. Chem , vol.264 , pp. 13873-13879
    • Bryan, J.1    Imai, M.2    Lee, R.3    Moore, P.4    Cook, R.G.5    Lin, W.G.6
  • 23
    • 0022974371 scopus 로고
    • The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin
    • Lash, J. A., Sellers, J. R., and Hathaway, D. R. (1986) The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin. J. Biol. Chem. 261, 16155-16160
    • (1986) J. Biol. Chem , vol.261 , pp. 16155-16160
    • Lash, J.A.1    Sellers, J.R.2    Hathaway, D.R.3
  • 24
    • 28044473860 scopus 로고    scopus 로고
    • The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable α-helix having unique electrostatic potential character
    • Liu, D., Yao, H., Chen, Y., Feng, Y., Chen, Y., and Wang, J. (2005) The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable α-helix having unique electrostatic potential character. Biochem. J. 392, 47-54
    • (2005) Biochem. J , vol.392 , pp. 47-54
    • Liu, D.1    Yao, H.2    Chen, Y.3    Feng, Y.4    Chen, Y.5    Wang, J.6
  • 26
    • 0031214378 scopus 로고    scopus 로고
    • An exceptionally stable helix from the ribosomal protein L9: Implications for protein folding and stability
    • Kuhlman, B., Yang, H. Y., Boice, J. A., Fairman, R., and Raleigh, D. P. (1997) An exceptionally stable helix from the ribosomal protein L9: implications for protein folding and stability. J. Mol. Biol. 270, 640-647
    • (1997) J. Mol. Biol , vol.270 , pp. 640-647
    • Kuhlman, B.1    Yang, H.Y.2    Boice, J.A.3    Fairman, R.4    Raleigh, D.P.5
  • 27
    • 44849116355 scopus 로고    scopus 로고
    • Long single α-helical tail domains bridge the gap between structure and function of myosin VI
    • Spink, B. J., Sivaramakrishnan, S., Lipfert, J., Doniach, S., and Spudich, J. A. (2008) Long single α-helical tail domains bridge the gap between structure and function of myosin VI. Nat. Struct. Mol. Biol. 15, 591-597
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 591-597
    • Spink, B.J.1    Sivaramakrishnan, S.2    Lipfert, J.3    Doniach, S.4    Spudich, J.A.5
  • 29
    • 72249096074 scopus 로고    scopus 로고
    • Combining single-molecule optical trapping and small-angle x-ray scattering measurements to compute the persistence length of a protein ER/K α-helix
    • Sivaramakrishnan, S., Sung, J., Ali, M., Doniach, S., Flyvbjerg, H., and Spudich, J. A. (2009) Combining single-molecule optical trapping and small-angle x-ray scattering measurements to compute the persistence length of a protein ER/K α-helix. Biophys. J. 97, 2993-2999
    • (2009) Biophys. J , vol.97 , pp. 2993-2999
    • Sivaramakrishnan, S.1    Sung, J.2    Ali, M.3    Doniach, S.4    Flyvbjerg, H.5    Spudich, J.A.6
  • 30
    • 70349266063 scopus 로고    scopus 로고
    • When a predicted coiled coil is really a single [small α]-helix, in myosins and other proteins
    • Peckham, M., and Knight, P. J. (2009) When a predicted coiled coil is really a single [small α]-helix, in myosins and other proteins. Soft Matter. 5, 2493-2503
    • (2009) Soft Matter , vol.5 , pp. 2493-2503
    • Peckham, M.1    Knight, P.J.2
  • 31
    • 61449257376 scopus 로고    scopus 로고
    • Charged single α-helix: A versatile protein structural motif
    • Süveges, D., Gáspári, Z., Tóth, G., and Nyitray, L. (2009) Charged single α-helix: a versatile protein structural motif. Proteins 74, 905-916
    • (2009) Proteins , vol.74 , pp. 905-916
    • Süveges, D.1    Gáspári, Z.2    Tóth, G.3    Nyitray, L.4
  • 32
    • 84857301203 scopus 로고    scopus 로고
    • Charged single α-helices in proteomes revealed by a consensus prediction approach
    • Gáspári, Z., Süveges, D., Perczel, A., Nyitray, L., and Tóth, G. (2012) Charged single α-helices in proteomes revealed by a consensus prediction approach. Biochim. Biophys. Acta 1824, 637-646
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 637-646
    • Gáspári, Z.1    Süveges, D.2    Perczel, A.3    Nyitray, L.4    Tóth, G.5
  • 34
    • 77956215275 scopus 로고    scopus 로고
    • Structured post-IQ domain governs selectivity of myosin X for fascin-actin bundles
    • Nagy, S., and Rock, R. S. (2010) Structured post-IQ domain governs selectivity of myosin X for fascin-actin bundles. J. Biol. Chem. 285, 26608-26617
    • (2010) J. Biol. Chem , vol.285 , pp. 26608-26617
    • Nagy, S.1    Rock, R.S.2
  • 35
    • 84896515379 scopus 로고    scopus 로고
    • Myosin lever arm directs collective motion on cellular actin network
    • Hariadi, R. F., Cale, M., and Sivaramakrishnan, S. (2014) Myosin lever arm directs collective motion on cellular actin network. Proc. Natl. Acad. Sci. U.S.A. 111, 4091-4096
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 4091-4096
    • Hariadi, R.F.1    Cale, M.2    Sivaramakrishnan, S.3
  • 36
    • 84855513111 scopus 로고    scopus 로고
    • Systematic control of protein interaction using a modular ER/K α-helix linker
    • Sivaramakrishnan, S., and Spudich, J. A. (2011) Systematic control of protein interaction using a modular ER/K α-helix linker. Proc. Natl. Acad. Sci. U.S.A. 108, 20467-20472
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 20467-20472
    • Sivaramakrishnan, S.1    Spudich, J.A.2
  • 37
    • 0032568591 scopus 로고    scopus 로고
    • Optimizing the stability of singlechain proteins by linker length and composition mutagenesis
    • Robinson, C. R., and Sauer, R. T. (1998) Optimizing the stability of singlechain proteins by linker length and composition mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 95, 5929-5934
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5929-5934
    • Robinson, C.R.1    Sauer, R.T.2
  • 38
    • 25144490502 scopus 로고    scopus 로고
    • How large is an α-helix? Studies of the radii of gyration of helical peptides by small-angle X-ray scattering and molecular dynamics
    • Zagrovic, B., Jayachandran, G., Millett, I. S., Doniach, S., and Pande, V. S. (2005) How large is an α-helix? Studies of the radii of gyration of helical peptides by small-angle X-ray scattering and molecular dynamics. J. Mol. Biol. 353, 232-241
    • (2005) J. Mol. Biol , vol.353 , pp. 232-241
    • Zagrovic, B.1    Jayachandran, G.2    Millett, I.S.3    Doniach, S.4    Pande, V.S.5
  • 39
    • 84879054442 scopus 로고    scopus 로고
    • Detection of G protein-selective G proteincoupled receptor (GPCR) conformations in live cells
    • Malik, R. U., Ritt, M., DeVree, B. T., Neubig, R. R., Sunahara, R. K., and Sivaramakrishnan, S. (2013) Detection of G protein-selective G proteincoupled receptor (GPCR) conformations in live cells. J. Biol. Chem. 288, 17167-17178
    • (2013) J. Biol. Chem , vol.288 , pp. 17167-17178
    • Malik, R.U.1    Ritt, M.2    Devree, B.T.3    Neubig, R.R.4    Sunahara, R.K.5    Sivaramakrishnan, S.6
  • 40
    • 84876000745 scopus 로고    scopus 로고
    • Visualizing and manipulating focal adhesion kinase regulation in live cells
    • Ritt, M., Guan, J. L., and Sivaramakrishnan, S. (2013) Visualizing and manipulating focal adhesion kinase regulation in live cells. J. Biol. Chem. 288, 8875-8886
    • (2013) J. Biol. Chem , vol.288 , pp. 8875-8886
    • Ritt, M.1    Guan, J.L.2    Sivaramakrishnan, S.3
  • 42
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • Kerppola, T. K. (2008) Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu. Rev. Biophys. 37, 465-487
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 43
    • 83055186516 scopus 로고    scopus 로고
    • Split-protein systems: Beyond binary protein-protein interactions
    • Shekhawat, S. S., and Ghosh, I. (2011) Split-protein systems: beyond binary protein-protein interactions. Curr. Opin. Chem. Biol. 15, 789-797
    • (2011) Curr. Opin. Chem. Biol , vol.15 , pp. 789-797
    • Shekhawat, S.S.1    Ghosh, I.2
  • 44
    • 84868556564 scopus 로고    scopus 로고
    • Optical control of protein activity by fluorescent protein domains
    • Zhou, X. X., Chung, H. K., Lam, A. J., and Lin, M. Z. (2012) Optical control of protein activity by fluorescent protein domains. Science 338, 810-814
    • (2012) Science , vol.338 , pp. 810-814
    • Zhou, X.X.1    Chung, H.K.2    Lam, A.J.3    Lin, M.Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.