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Volumn 373, Issue 2, 2007, Pages 476-490

The Rough Energy Landscape of Superfolder GFP Is Linked to the Chromophore

Author keywords

free energy landscape; hysteresis; post translational modification; protein folding; barrel

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 34548816178     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.07.071     Document Type: Article
Times cited : (67)

References (85)
  • 1
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67 (1998) 509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 2
    • 0141888960 scopus 로고    scopus 로고
    • Improving protein folding efficiency by directed evolution using the GFP folding reporter
    • Waldo G.S. Improving protein folding efficiency by directed evolution using the GFP folding reporter. Methods Mol. Biol. 230 (2003) 343-359
    • (2003) Methods Mol. Biol. , vol.230 , pp. 343-359
    • Waldo, G.S.1
  • 4
    • 26444492138 scopus 로고    scopus 로고
    • Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis
    • Cabantous S., Pedelacq J.D., Mark B.L., Naranjo C., Terwilliger T.C., and Waldo G.S. Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis. J. Struct. Funct. Genom. 6 (2005) 113-119
    • (2005) J. Struct. Funct. Genom. , vol.6 , pp. 113-119
    • Cabantous, S.1    Pedelacq, J.D.2    Mark, B.L.3    Naranjo, C.4    Terwilliger, T.C.5    Waldo, G.S.6
  • 5
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous S., Terwilliger T.C., and Waldo G.S. Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nature Biotechnol. 23 (2005) 102-107
    • (2005) Nature Biotechnol. , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 6
    • 24144454858 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with GFP-fragment reassembly
    • Wilson C.G., Magliery T.J., and Regan L. Detecting protein-protein interactions with GFP-fragment reassembly. Nature Methods 1 (2004) 255-262
    • (2004) Nature Methods , vol.1 , pp. 255-262
    • Wilson, C.G.1    Magliery, T.J.2    Regan, L.3
  • 7
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism
    • Magliery T.J., Wilson C.G., Pan W., Mishler D., Ghosh I., Hamilton A.D., and Regan L. Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J. Am. Chem. Soc. 127 (2005) 146-157
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.2    Pan, W.3    Mishler, D.4    Ghosh, I.5    Hamilton, A.D.6    Regan, L.7
  • 8
    • 0030595059 scopus 로고    scopus 로고
    • Quantitative analysis of transient gene expression in mammalian cells using the green fluorescent protein
    • Subramanian S., and Srienc F. Quantitative analysis of transient gene expression in mammalian cells using the green fluorescent protein. J. Biotechnol. 49 (1996) 137-151
    • (1996) J. Biotechnol. , vol.49 , pp. 137-151
    • Subramanian, S.1    Srienc, F.2
  • 9
    • 0038054074 scopus 로고    scopus 로고
    • Development and application of unstable GFP variants to kinetic studies of mycobacterial gene expression
    • Blokpoel M.C., O'Toole R., Smeulders M.J., and Williams H.D. Development and application of unstable GFP variants to kinetic studies of mycobacterial gene expression. J. Microbiol. Methods 54 (2003) 203-211
    • (2003) J. Microbiol. Methods , vol.54 , pp. 203-211
    • Blokpoel, M.C.1    O'Toole, R.2    Smeulders, M.J.3    Williams, H.D.4
  • 10
    • 0035875010 scopus 로고    scopus 로고
    • Ordering genes in a flagella pathway by analysis of expression kinetics from living bacteria
    • Kalir S., McClure J., Pabbaraju K., Southward C., Ronen M., Leibler S., et al. Ordering genes in a flagella pathway by analysis of expression kinetics from living bacteria. Science 292 (2001) 2080-2083
    • (2001) Science , vol.292 , pp. 2080-2083
    • Kalir, S.1    McClure, J.2    Pabbaraju, K.3    Southward, C.4    Ronen, M.5    Leibler, S.6
  • 11
    • 10044236579 scopus 로고    scopus 로고
    • A high-throughput approach to promoter study using green fluorescent protein
    • Lu C., Bentley W.E., and Rao G. A high-throughput approach to promoter study using green fluorescent protein. Biotechnol. Prog. 20 (2004) 1634-1640
    • (2004) Biotechnol. Prog. , vol.20 , pp. 1634-1640
    • Lu, C.1    Bentley, W.E.2    Rao, G.3
  • 12
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid B.G., and Flynn G.C. Chromophore formation in green fluorescent protein. Biochemistry 36 (1997) 6786-6791
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 13
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • Fukuda H., Arai M., and Kuwajima K. Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 39 (2000) 12025-12032
    • (2000) Biochemistry , vol.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 14
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri A., Whitehorn E.A., Tate E., and Stemmer W.P. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nature Biotechnol. 14 (1996) 315-319
    • (1996) Nature Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 15
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack B.P., Valdivia R.H., and Falkow S. FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173 (1996) 33-38
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 16
    • 8344290520 scopus 로고    scopus 로고
    • Acid denaturation and refolding of green fluorescent protein
    • Enoki S., Saeki K., Maki K., and Kuwajima K. Acid denaturation and refolding of green fluorescent protein. Biochemistry 43 (2004) 14238-14248
    • (2004) Biochemistry , vol.43 , pp. 14238-14248
    • Enoki, S.1    Saeki, K.2    Maki, K.3    Kuwajima, K.4
  • 19
    • 0037304389 scopus 로고    scopus 로고
    • Genetic screens and directed evolution for protein solubility
    • Waldo G.S. Genetic screens and directed evolution for protein solubility. Curr. Opin. Chem. Biol. 7 (2003) 33-38
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 33-38
    • Waldo, G.S.1
  • 22
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., and Prasher D.C. Green fluorescent protein as a marker for gene expression. Science 263 (1994) 802-805
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 24
    • 0023517017 scopus 로고
    • Effect of point mutations on the folding of globular proteins
    • Matthews C.R. Effect of point mutations on the folding of globular proteins. Methods Enzymol. 154 (1987) 498-511
    • (1987) Methods Enzymol. , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 25
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin-1 beta
    • Heidary D.K., Gross L.A., Roy M., and Jennings P.A. Evidence for an obligatory intermediate in the folding of interleukin-1 beta. Nature Struct. Biol. 4 (1997) 725-731
    • (1997) Nature Struct. Biol. , vol.4 , pp. 725-731
    • Heidary, D.K.1    Gross, L.A.2    Roy, M.3    Jennings, P.A.4
  • 27
    • 33746911626 scopus 로고    scopus 로고
    • The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein
    • Enoki S., Maki K., Inobe T., Takahashi K., Kamagata K., Oroguchi T., et al. The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein. J. Mol. Biol. 361 (2006) 969-982
    • (2006) J. Mol. Biol. , vol.361 , pp. 969-982
    • Enoki, S.1    Maki, K.2    Inobe, T.3    Takahashi, K.4    Kamagata, K.5    Oroguchi, T.6
  • 28
    • 2542494929 scopus 로고    scopus 로고
    • Unification of the folding mechanisms of non-two-state and two-state proteins
    • Kamagata K., Arai M., and Kuwajima K. Unification of the folding mechanisms of non-two-state and two-state proteins. J. Mol. Biol. 339 (2004) 951-965
    • (2004) J. Mol. Biol. , vol.339 , pp. 951-965
    • Kamagata, K.1    Arai, M.2    Kuwajima, K.3
  • 29
    • 0016711868 scopus 로고
    • Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts J.F., Halvorson H.R., and Brennan M. Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14 (1975) 4953-4963
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 30
    • 14944346760 scopus 로고    scopus 로고
    • Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains
    • Krieger F., Moglich A., and Kiefhaber T. Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains. J. Am. Chem. Soc. 127 (2005) 3346-3352
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 3346-3352
    • Krieger, F.1    Moglich, A.2    Kiefhaber, T.3
  • 31
    • 0025195733 scopus 로고
    • Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization
    • Kiefhaber T., Quaas R., Hahn U., and Schmid F.X. Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry 29 (1990) 3053-3061
    • (1990) Biochemistry , vol.29 , pp. 3053-3061
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 32
    • 0027049568 scopus 로고
    • Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation
    • Schultz D.A., Schmid F.X., and Baldwin R.L. Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci. 1 (1992) 917-924
    • (1992) Protein Sci. , vol.1 , pp. 917-924
    • Schultz, D.A.1    Schmid, F.X.2    Baldwin, R.L.3
  • 33
    • 0343617266 scopus 로고
    • On the production of transient electric currents in iron and steel conductors by twisting them when magnetised, or by magnetising them when twisted
    • Ewing J.A. On the production of transient electric currents in iron and steel conductors by twisting them when magnetised, or by magnetising them when twisted. Proc. Roy. Soc. London 36 (1883) 117-135
    • (1883) Proc. Roy. Soc. London , vol.36 , pp. 117-135
    • Ewing, J.A.1
  • 34
    • 33750612930 scopus 로고    scopus 로고
    • Understanding the folding of GFP using biophysical techniques
    • Jackson S.E., Craggs T.D., and Huang J.R. Understanding the folding of GFP using biophysical techniques. Expert. Rev. Proteom. 3 (2006) 545-559
    • (2006) Expert. Rev. Proteom. , vol.3 , pp. 545-559
    • Jackson, S.E.1    Craggs, T.D.2    Huang, J.R.3
  • 35
    • 34249657467 scopus 로고    scopus 로고
    • Stable intermediate states and high energy barriers in the unfolding of GFP
    • Huang J.R., Craggs T.D., Christodoulou J., and Jackson S.E. Stable intermediate states and high energy barriers in the unfolding of GFP. J. Mol. Biol. 370 (2007) 356-371
    • (2007) J. Mol. Biol. , vol.370 , pp. 356-371
    • Huang, J.R.1    Craggs, T.D.2    Christodoulou, J.3    Jackson, S.E.4
  • 36
    • 0035879166 scopus 로고    scopus 로고
    • Photoisomerization of green fluorescent protein and the dimensions of the chromophore cavity
    • Chen M.C., Lambert C.R., Urgitis J.D., and Zimmer M. Photoisomerization of green fluorescent protein and the dimensions of the chromophore cavity. Chem. Phys. 270 (2001) 157-164
    • (2001) Chem. Phys. , vol.270 , pp. 157-164
    • Chen, M.C.1    Lambert, C.R.2    Urgitis, J.D.3    Zimmer, M.4
  • 37
    • 13544256284 scopus 로고    scopus 로고
    • Understanding GFP chromophore biosynthesis: controlling backbone cyclization and modifying post-translational chemistry
    • Barondeau D.P., Kassmann C.J., Tainer J.A., and Getzoff E.D. Understanding GFP chromophore biosynthesis: controlling backbone cyclization and modifying post-translational chemistry. Biochemistry 44 (2005) 1960-1970
    • (2005) Biochemistry , vol.44 , pp. 1960-1970
    • Barondeau, D.P.1    Kassmann, C.J.2    Tainer, J.A.3    Getzoff, E.D.4
  • 38
    • 0001663148 scopus 로고    scopus 로고
    • Energetic and thermodynamic aspects of hysteresis
    • Bertotti G. Energetic and thermodynamic aspects of hysteresis. Phys. Rev. Letters 76 (1996) 1739-1742
    • (1996) Phys. Rev. Letters , vol.76 , pp. 1739-1742
    • Bertotti, G.1
  • 41
    • 0030874395 scopus 로고    scopus 로고
    • Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers
    • Lai Z., McCulloch J., Lashuel H.A., and Kelly J.W. Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers. Biochemistry 36 (1997) 10230-10239
    • (1997) Biochemistry , vol.36 , pp. 10230-10239
    • Lai, Z.1    McCulloch, J.2    Lashuel, H.A.3    Kelly, J.W.4
  • 42
    • 28844435014 scopus 로고    scopus 로고
    • Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu, Zn superoxide dismutases
    • Rumfeldt J.A., Stathopulos P.B., Chakrabarrty A., Lepock J.R., and Meiering E.M. Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu, Zn superoxide dismutases. J. Mol. Biol. 355 (2006) 106-123
    • (2006) J. Mol. Biol. , vol.355 , pp. 106-123
    • Rumfeldt, J.A.1    Stathopulos, P.B.2    Chakrabarrty, A.3    Lepock, J.R.4    Meiering, E.M.5
  • 43
    • 0027162959 scopus 로고
    • Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits
    • Clark A.C., Sinclair J.F., and Baldwin T.O. Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits. J. Biol. Chem. 268 (1993) 10773-10779
    • (1993) J. Biol. Chem. , vol.268 , pp. 10773-10779
    • Clark, A.C.1    Sinclair, J.F.2    Baldwin, T.O.3
  • 44
    • 0035979373 scopus 로고    scopus 로고
    • Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: evidence of dimerization coupled to refolding of the thermally unfolded protein
    • Benitez-Cardoza C.G., Rojo-Dominguez A., and Hernandez-Arana A. Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: evidence of dimerization coupled to refolding of the thermally unfolded protein. Biochemistry 40 (2001) 9049-9058
    • (2001) Biochemistry , vol.40 , pp. 9049-9058
    • Benitez-Cardoza, C.G.1    Rojo-Dominguez, A.2    Hernandez-Arana, A.3
  • 45
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva A., Kulke M., Fernandez J.M., and Linke W.A. Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys. J. 80 (2001) 1442-14451
    • (2001) Biophys. J. , vol.80 , pp. 1442-14451
    • Minajeva, A.1    Kulke, M.2    Fernandez, J.M.3    Linke, W.A.4
  • 47
    • 0027491607 scopus 로고
    • Hysteresis in the triple helix-coil transition of type III collagen
    • Davis J.M., and Bachinger H.P. Hysteresis in the triple helix-coil transition of type III collagen. J. Biol. Chem. 268 (1993) 25965-25972
    • (1993) J. Biol. Chem. , vol.268 , pp. 25965-25972
    • Davis, J.M.1    Bachinger, H.P.2
  • 48
    • 0342588050 scopus 로고    scopus 로고
    • Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding
    • Engel J., and Bachinger H.P. Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. Matrix Biol. 19 (2000) 235-244
    • (2000) Matrix Biol. , vol.19 , pp. 235-244
    • Engel, J.1    Bachinger, H.P.2
  • 49
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi C., Shank E.A., Bustamante C., and Marqusee S. Direct observation of the three-state folding of a single protein molecule. Science 309 (2005) 2057-2060
    • (2005) Science , vol.309 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 50
    • 9244234443 scopus 로고    scopus 로고
    • Exploring the energy landscape of GFP by single-molecule mechanical experiments
    • Dietz H., and Rief M. Exploring the energy landscape of GFP by single-molecule mechanical experiments. Proc. Natl Acad. Sci. USA 101 (2004) 16192-16197
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 16192-16197
    • Dietz, H.1    Rief, M.2
  • 51
    • 33748046806 scopus 로고    scopus 로고
    • Anisotropic deformation response of single protein molecules
    • Dietz H., Berkemeier F., Bertz M., and Rief M. Anisotropic deformation response of single protein molecules. Proc. Natl Acad. Sci. USA 103 (2007) 12724-12728
    • (2007) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12724-12728
    • Dietz, H.1    Berkemeier, F.2    Bertz, M.3    Rief, M.4
  • 53
    • 0036166211 scopus 로고    scopus 로고
    • Irreversible assembly of membrane fusion machines
    • Barrick D., and Hughson F.M. Irreversible assembly of membrane fusion machines. Nature Struct. Biol. 9 (2002) 78-80
    • (2002) Nature Struct. Biol. , vol.9 , pp. 78-80
    • Barrick, D.1    Hughson, F.M.2
  • 54
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain A.K., Handel T.M., and Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Struct. Biol. 3 (1996) 782-787
    • (1996) Nature Struct. Biol. , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 58
    • 33747592347 scopus 로고    scopus 로고
    • The experimental survey of protein-folding energy landscapes
    • Oliveberg M., and Wolynes P.G. The experimental survey of protein-folding energy landscapes. Quart. Rev. Biophys. 38 (2005) 245-288
    • (2005) Quart. Rev. Biophys. , vol.38 , pp. 245-288
    • Oliveberg, M.1    Wolynes, P.G.2
  • 59
  • 60
    • 0142027791 scopus 로고    scopus 로고
    • Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures
    • Barondeau D.P., Putnam C.D., Kassmann C.J., Tainer J.A., and Getzoff E.D. Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures. Proc. Natl Acad. Sci. USA 100 (2003) 12111-12116
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12111-12116
    • Barondeau, D.P.1    Putnam, C.D.2    Kassmann, C.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 63
    • 11844250759 scopus 로고    scopus 로고
    • The crystal structure of the Y66L variant of green fluorescent protein supports a cyclization-oxidation-dehydration mechanism for chromophore maturation
    • Rosenow M.A., Huffman H.A., Phail M.E., and Wachter R.M. The crystal structure of the Y66L variant of green fluorescent protein supports a cyclization-oxidation-dehydration mechanism for chromophore maturation. Biochemistry 43 (2004) 4464-4472
    • (2004) Biochemistry , vol.43 , pp. 4464-4472
    • Rosenow, M.A.1    Huffman, H.A.2    Phail, M.E.3    Wachter, R.M.4
  • 64
    • 0035152671 scopus 로고    scopus 로고
    • Theoretical study of the mechanism of peptide ring formation in green fluorescent protein
    • Siegbahn P.E.M., Wirstam M., and Zimmer M. Theoretical study of the mechanism of peptide ring formation in green fluorescent protein. Internat. J. Quantum Chem. 81 (2000) 169-186
    • (2000) Internat. J. Quantum Chem. , vol.81 , pp. 169-186
    • Siegbahn, P.E.M.1    Wirstam, M.2    Zimmer, M.3
  • 65
    • 33646240062 scopus 로고    scopus 로고
    • The role of the protein matrix in green fluorescent protein fluorescence
    • Maddalo S.L., and Zimmer M. The role of the protein matrix in green fluorescent protein fluorescence. Photochem. Photobiol. 82 (2006) 367-372
    • (2006) Photochem. Photobiol. , vol.82 , pp. 367-372
    • Maddalo, S.L.1    Zimmer, M.2
  • 66
    • 10844242118 scopus 로고    scopus 로고
    • Molecular modeling of green fluorescent protein: structural effects of chromophore deprotonation
    • Patnaik S.S., Trohalaki S., and Pachter R. Molecular modeling of green fluorescent protein: structural effects of chromophore deprotonation. Biopolymers 75 (2004) 441-452
    • (2004) Biopolymers , vol.75 , pp. 441-452
    • Patnaik, S.S.1    Trohalaki, S.2    Pachter, R.3
  • 67
    • 34249844859 scopus 로고    scopus 로고
    • Structural basis for reversible photobleaching of a green fluorescent protein homologue
    • Henderson J.N., Ai H.W., Campbell R.E., and Remington S.J. Structural basis for reversible photobleaching of a green fluorescent protein homologue. Proc. Natl Acad. Sci. USA 104 (2007) 6672-6677
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 6672-6677
    • Henderson, J.N.1    Ai, H.W.2    Campbell, R.E.3    Remington, S.J.4
  • 70
    • 0026723063 scopus 로고
    • Protein folding funnels- a kinetic approach to the sequence structure relationship
    • Leopold P.E., Montal M., and Onuchic J.N. Protein folding funnels- a kinetic approach to the sequence structure relationship. Proc. Natl Acad. Sci. USA 89 (1992) 8721-8725
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 73
    • 0028774340 scopus 로고
    • Stability and function-2 constraints in the evolution of Barstar and other proteins
    • Schreiber C., Buckle A.M., and Fersht A.R. Stability and function-2 constraints in the evolution of Barstar and other proteins. Structure 2 (1994) 945-951
    • (1994) Structure , vol.2 , pp. 945-951
    • Schreiber, C.1    Buckle, A.M.2    Fersht, A.R.3
  • 75
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang W.Y., and Gruebele M. Folding at the speed limit. Nature 423 (2003) 193-197
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 76
    • 33745931359 scopus 로고    scopus 로고
    • Multiple routes lead to the native state in the energy landscape of the beta-trefoil family
    • Chavez L.L., Gosavi S., Jennings P.A., and Onuchic J.N. Multiple routes lead to the native state in the energy landscape of the beta-trefoil family. Proc. Natl Acad. Sci. USA 103 (2006) 10254-10258
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10254-10258
    • Chavez, L.L.1    Gosavi, S.2    Jennings, P.A.3    Onuchic, J.N.4
  • 77
    • 33645030244 scopus 로고    scopus 로고
    • Topological frustration and the folding of interleukin-1 beta
    • Gosavi S., Chavez L.L., Jennings P.A., and Onuchic J.N. Topological frustration and the folding of interleukin-1 beta. J. Mol. Biol. 357 (2006) 986-996
    • (2006) J. Mol. Biol. , vol.357 , pp. 986-996
    • Gosavi, S.1    Chavez, L.L.2    Jennings, P.A.3    Onuchic, J.N.4
  • 78
    • 0242268469 scopus 로고    scopus 로고
    • Non-linear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins
    • Miyashita O., Onuchic J.N., and Wolynes P.G. Non-linear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins. Proc. Natl Acad. Sci. USA 100 (2003) 12570-12575
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12570-12575
    • Miyashita, O.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 79
    • 13444305369 scopus 로고    scopus 로고
    • Simple energy landscape model for the kinetics of functional transitions in proteins
    • Miyashita O., Wolynes P.G., and Onuchic J.N. Simple energy landscape model for the kinetics of functional transitions in proteins. J. Phys. Chem. ser. B 109 (2005) 1959-1969
    • (2005) J. Phys. Chem. ser. B , vol.109 , pp. 1959-1969
    • Miyashita, O.1    Wolynes, P.G.2    Onuchic, J.N.3
  • 80
    • 33749071408 scopus 로고    scopus 로고
    • Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding
    • Petrescu A.J., Wormald M.R., and Dwek R.A. Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding. Curr. Opin. Struct. Biol. 16 (2006) 600-607
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 600-607
    • Petrescu, A.J.1    Wormald, M.R.2    Dwek, R.A.3
  • 82
    • 24644442164 scopus 로고    scopus 로고
    • The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain
    • Shen T., Zong C., Hamelberg D., McCammon J.A., and Wolynes P.G. The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain. FASEB J. 19 (2005) 1389-1395
    • (2005) FASEB J. , vol.19 , pp. 1389-1395
    • Shen, T.1    Zong, C.2    Hamelberg, D.3    McCammon, J.A.4    Wolynes, P.G.5
  • 83
    • 0035128033 scopus 로고    scopus 로고
    • Energy landscapes of conformationally constrained peptides
    • Levy Y., and Becker O.M. Energy landscapes of conformationally constrained peptides. J. Chem. Phys. 114 (2001) 993-1009
    • (2001) J. Chem. Phys. , vol.114 , pp. 993-1009
    • Levy, Y.1    Becker, O.M.2
  • 84
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous-solutions
    • Piotto M., Saudek V., and Sklenar V. Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous-solutions. J. Biomol. NMR 2 (1992) 661-665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 85
    • 0001350902 scopus 로고
    • Gradient-tailored water suppression for H-1-N-15 HSQC experiments optimized to retain full sensitivity
    • Sklenar V., Piotto M., Leppik R., and Saudek V. Gradient-tailored water suppression for H-1-N-15 HSQC experiments optimized to retain full sensitivity. J. Mag. Reson. ser. A 102 (1993) 241-245
    • (1993) J. Mag. Reson. ser. A , vol.102 , pp. 241-245
    • Sklenar, V.1    Piotto, M.2    Leppik, R.3    Saudek, V.4


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