메뉴 건너뛰기




Volumn 288, Issue 4, 1999, Pages 743-752

Helix capping in the GCN4 leucine zipper

Author keywords

Coiled coil; GCN4 leucine zipper; Helix capping; Protein folding; Thermal stability

Indexed keywords

LEUCINE ZIPPER PROTEIN;

EID: 0033006632     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2707     Document Type: Article
Times cited : (39)

References (65)
  • 2
    • 0026696173 scopus 로고
    • Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr59
    • Bell J. A., Beckel W. J., Sauer U., Baase W. A., Matthews B. M. Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr59. Biochemistry. 31:1992;3590-3596.
    • (1992) Biochemistry , vol.31 , pp. 3590-3596
    • Bell, J.A.1    Beckel, W.J.2    Sauer, U.3    Baase, W.A.4    Matthews, B.M.5
  • 6
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen Y.-H., Yang J. T., Chau K. H. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry. 13:1974;3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 7
    • 0028293441 scopus 로고
    • Alpha-helical coiled coils: More facts and better predictions
    • Cohen C., Parry D. A. Alpha-helical coiled coils: more facts and better predictions. Science. 263:1994;488-489.
    • (1994) Science , vol.263 , pp. 488-489
    • Cohen, C.1    Parry, D.A.2
  • 8
    • 0025130161 scopus 로고
    • Structural features in the heptad substructure and longer range repeats of two-stranded α-fibrous proteins
    • Conway J. F., Parry D. A. Structural features in the heptad substructure and longer range repeats of two-stranded α-fibrous proteins. Int. J. Biol. Macromol. 12:1990;328-334.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.2
  • 9
    • 0027212028 scopus 로고
    • Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions
    • Dasgupta S., Bell J. A. Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions. Int. J. Pept. Protein Res. 41:1993;499-511.
    • (1993) Int. J. Pept. Protein Res. , vol.41 , pp. 499-511
    • Dasgupta, S.1    Bell, J.A.2
  • 10
    • 0029020484 scopus 로고
    • N- And C-capping preferences for all 20 amino acids in α helical peptides
    • Doig A. J., Baldwin R. L. N- and C-capping preferences for all 20 amino acids in α helical peptides. Protein Sci. 4:1995;1325-1336.
    • (1995) Protein Sci. , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 11
    • 0028289435 scopus 로고
    • Determination of free energies of N capping in alpha helices by modification of the Lifson-Roig helix coil theory to include N- And C-capping
    • Doig A. J., Chakrabartty A., Klingler T. M., Baldwin R. L. Determination of free energies of N capping in alpha helices by modification of the Lifson-Roig helix coil theory to include N- and C-capping. Biochemistry. 33:1994;3396-3403.
    • (1994) Biochemistry , vol.33 , pp. 3396-3403
    • Doig, A.J.1    Chakrabartty, A.2    Klingler, T.M.3    Baldwin, R.L.4
  • 12
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 6:1967;1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 13
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S. V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 14
    • 0027404071 scopus 로고
    • Stabilization of helical structure in short peptides via capping
    • Forood B., Feliciano E. J., Nambiar K. P. Stabilization of helical structure in short peptides via capping. Proc. Natl Acad. Sci. USA. 90:1994;838-842.
    • (1994) Proc. Natl Acad. Sci. USA , vol.90 , pp. 838-842
    • Forood, B.1    Feliciano, E.J.2    Nambiar, K.P.3
  • 15
    • 0029081270 scopus 로고
    • Structural analysis of the N- And C-termini in a peptide with consensus sequence
    • Gong Y., Zhou H. X., Guo M., Kallenbach N. R. Structural analysis of the N- and C-termini in a peptide with consensus sequence. Protein Sci. 4:1995;1446-1456.
    • (1995) Protein Sci. , vol.4 , pp. 1446-1456
    • Gong, Y.1    Zhou, H.X.2    Guo, M.3    Kallenbach, N.R.4
  • 16
    • 0026317334 scopus 로고
    • Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide
    • Goodman E. M., Kim P. S. Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide. Biochemistry. 30:1991;11615-11620.
    • (1991) Biochemistry , vol.30 , pp. 11615-11620
    • Goodman, E.M.1    Kim, P.S.2
  • 17
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P. B., Zhang T., Kim P. S., Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 18
    • 0027204024 scopus 로고
    • Helix stop signal in proteins and peptides: The capping box
    • Harper E., Rose G. D. Helix stop signal in proteins and peptides: the capping box. Biochemistry. 32:1993;7605-7609.
    • (1993) Biochemistry , vol.32 , pp. 7605-7609
    • Harper, E.1    Rose, G.D.2
  • 19
    • 0013880887 scopus 로고
    • Experimental free energy and enthalpy of formation of the α helix
    • Hermans J. Jr. Experimental free energy and enthalpy of formation of the α helix. J. Phys. Chem. 70:1966;510-515.
    • (1966) J. Phys. Chem. , vol.70 , pp. 510-515
    • Hermans J., Jr.1
  • 21
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson M. L., Correia J. J., Yphantis D. A., Halvorson H. R. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:1981;575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J.-Y., Cowan S. W. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3
  • 23
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1982;631-660.
    • (1982) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 24
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 25
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S. E. Harding, A. J. Rowe, & J. C. Horton. Cambridge: Royal Society of Chemistry
    • Laue T. M., Shah B. D., Ridgeway T. M., Pelletier S. L. Computer-aided interpretation of analytical sedimentation data for proteins. Harding S. E., Rowe A. J., Horton J. C. Analytical Ultracentrifugation in Biochemistry and Polymer Science. 1992;90-125 Royal Society of Chemistry, Cambridge.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 26
    • 0018093765 scopus 로고
    • Conformational preferences of amino acids in globular proteins
    • Levitt M. Conformational preferences of amino acids in globular proteins. Biochemistry. 17:1978;4277-4285.
    • (1978) Biochemistry , vol.17 , pp. 4277-4285
    • Levitt, M.1
  • 28
    • 0032899254 scopus 로고    scopus 로고
    • Subdomain folding and biological activity of the core structure from HIV-1 gp41: Implications for viral membrane fusion
    • Lu M., Ji H., Shen S. Subdomain folding and biological activity of the core structure from HIV-1 gp41: implications for viral membrane fusion. J. Virol. 173:1999;4433-4438.
    • (1999) J. Virol. , vol.173 , pp. 4433-4438
    • Lu, M.1    Ji, H.2    Shen, S.3
  • 29
    • 0029030233 scopus 로고
    • Measurement of interhelical elctrostatic interactions in the GCN4 leucine zipper
    • Lumb K. J., Kim P. S. Measurement of interhelical elctrostatic interactions in the GCN4 leucine zipper. Science. 268:1995;436-439.
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 30
    • 0028306360 scopus 로고
    • Subdomain folding of the coiled coil leucine zipper from the transcriptional activator GCN4
    • Lumb K. J., Carr C. M., Kim P. S. Subdomain folding of the coiled coil leucine zipper from the transcriptional activator GCN4. Biochemistry. 33:1994;7361-7367.
    • (1994) Biochemistry , vol.33 , pp. 7361-7367
    • Lumb, K.J.1    Carr, C.M.2    Kim, P.S.3
  • 31
    • 0027391780 scopus 로고
    • Capping interactions in isolated α helices: Position dependent substitution effects and structure of a serine capped peptide helix
    • Lyu P. C., Wemmer D. E., Zhou H. X., Pinker R. J., Kallenbach N. R. Capping interactions in isolated α helices: position dependent substitution effects and structure of a serine capped peptide helix. Biochemistry. 32:1993;421-425.
    • (1993) Biochemistry , vol.32 , pp. 421-425
    • Lyu, P.C.1    Wemmer, D.E.2    Zhou, H.X.3    Pinker, R.J.4    Kallenbach, N.R.5
  • 32
    • 0028968018 scopus 로고
    • Studies on protein stability with T4 lysozyme
    • Matthews B. W. Studies on protein stability with T4 lysozyme. Advan. Protein Chem. 46:1995;249-278.
    • (1995) Advan. Protein Chem. , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 33
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan A. D., Stewart M. Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98:1975;293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 34
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled coils
    • Monera O. D., Kay C. M., Hodges R. S. . Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled coils. Biochemistry. 33:1994;3862-3871.
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 35
    • 0029009067 scopus 로고
    • The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding
    • Munoz V., Blanco F. J., Serrano L. The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding. Nature Struct. Biol. 2:1995;380-385.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 380-385
    • Munoz, V.1    Blanco, F.J.2    Serrano, L.3
  • 36
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 37
    • 0023692599 scopus 로고
    • A peptide model of a protein folding intermediate
    • Oas T. G., Kim P. S. A peptide model of a protein folding intermediate. Nature. 336:1988;42-48.
    • (1988) Nature , vol.336 , pp. 42-48
    • Oas, T.G.1    Kim, P.S.2
  • 38
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil K. T., DeGrado W. F. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250:1990;646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 39
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea E. K., Rutkowski R., Kim P. S. Evidence that the leucine zipper is a coiled coil. Science. 243:1989;538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 40
    • 0026331267 scopus 로고
    • A. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel, coiled coil
    • O'Shea E. K., Klemm J. D., Kim P. S., Alber T. A. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel, coiled coil. Science. 254:1991;539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 41
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • O'Shea E. K., Rutkowski R., Kim P. S. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell. 66:1992;699-708.
    • (1992) Cell , vol.66 , pp. 699-708
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1996;307-326.
    • (1996) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0003621450 scopus 로고
    • New York: Dover Publications Inc.
    • Pauling L. General Chemistry. 1970;Dover Publications Inc. New York.
    • (1970) General Chemistry
    • Pauling, L.1
  • 44
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling L., Corey R. B., Branson H. R. The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl Acad. Sci. USA. 37:1951;205-210.
    • (1951) Proc. Natl Acad. Sci. USA , vol.37 , pp. 205-210
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 45
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta L. G., Rose G. D. Helix signals in proteins. Science. 240:1988;1632-1641.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 46
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helices
    • Richardson J. S., Richardson D. C. Amino acid preferences for specific locations at the ends of α helices. Science. 240:1988;1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 49
    • 0027986703 scopus 로고
    • Sequence determinants of the capping box, a stabilizing motif at the N-termini of α helices
    • Seale J. W., Srinivasan R., Rose G. D. Sequence determinants of the capping box, a stabilizing motif at the N-termini of α helices. Protein Sci. 3:1994;1741-1745.
    • (1994) Protein Sci. , vol.3 , pp. 1741-1745
    • Seale, J.W.1    Srinivasan, R.2    Rose, G.D.3
  • 50
    • 0024972479 scopus 로고
    • Capping and α-helix stability
    • Serrano L., Fersht A. R. Capping and α-helix stability. Nature. 342:1989;296-299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 51
    • 0026516310 scopus 로고
    • Effect of alanine versus glycine in α-helices on protein stability
    • Serrano L., Neira J.-L., Sancho J., Fersht A. R. Effect of alanine versus glycine in α-helices on protein stability. Nature. 356:1992;453-455.
    • (1992) Nature , vol.356 , pp. 453-455
    • Serrano, L.1    Neira, J.-L.2    Sancho, J.3    Fersht, A.R.4
  • 52
    • 0027248899 scopus 로고
    • Peptide models of protein folding initiation sites. 2. The G-H helical hairpin of myoglobin
    • Shin H. C., Merutka G., Waltho J. P., Tennant L. L., Dyson H. J., Wright P. E. Peptide models of protein folding initiation sites. 2. The G-H helical hairpin of myoglobin. Biochemistry. 32:1993a;6356-6364.
    • (1993) Biochemistry , vol.32 , pp. 6356-6364
    • Shin, H.C.1    Merutka, G.2    Waltho, J.P.3    Tennant, L.L.4    Dyson, H.J.5    Wright, P.E.6
  • 53
    • 0027165689 scopus 로고
    • Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal
    • Shin H. C., Merutka G., Waltho J. P., Wright P. E., Dyson H. J. Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal. Biochemistry. 32:1993b;6348-6355.
    • (1993) Biochemistry , vol.32 , pp. 6348-6355
    • Shin, H.C.1    Merutka, G.2    Waltho, J.P.3    Wright, P.E.4    Dyson, H.J.5
  • 54
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for stabilization of α helices
    • Shoemaker K. R., Kim P. S., York E. J., Stewart J. M., Baldwin R. L. Tests of the helix dipole model for stabilization of α helices. Nature. 326:1989;563-567.
    • (1989) Nature , vol.326 , pp. 563-567
    • Shoemaker, K.R.1    Kim, P.S.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 55
    • 0029055313 scopus 로고
    • LINUS: A hierarchic approach to predict the fold of a protein
    • Srinivasan R., Rose G. D. LINUS: a hierarchic approach to predict the fold of a protein. Proteins: Struct. Funct. Genet. 22:1995;81-99.
    • (1995) Proteins: Struct. Funct. Genet. , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2
  • 57
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thompson K. S., Vinson C. R., Freire E. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry. 32:1993;5491-5496.
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 58
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites. 1. Secondary structure formation in peptides corresponding to the G- And H- helices of myoglobin
    • Waltho P. J., Feher V. A., Merutka G. D., Dyson H. J., Wright P. E. Peptide models of protein folding initiation sites. 1. Secondary structure formation in peptides corresponding to the G- and H- helices of myoglobin. Biochemistry. 32:1993;6337-6347.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, P.J.1    Feher, V.A.2    Merutka, G.D.3    Dyson, H.J.4    Wright, P.E.5
  • 59
    • 0029083811 scopus 로고
    • Predicting oligomerization states of coiled coils
    • Woolfson D. N., Alber T. Predicting oligomerization states of coiled coils. Protein Sci. 4:1995;1596-1607.
    • (1995) Protein Sci. , vol.4 , pp. 1596-1607
    • Woolfson, D.N.1    Alber, T.2
  • 60
    • 0032556223 scopus 로고    scopus 로고
    • α-helix nucleation constant in copolypeptides of alanine and ornithine or lysine
    • Yang J., Zhao K., Gong Y., Vologodskii A., Kallenbach N. R. α-helix nucleation constant in copolypeptides of alanine and ornithine or lysine. J. Am. Chem. Soc. 120:1998;10646-10652.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10646-10652
    • Yang, J.1    Zhao, K.2    Gong, Y.3    Vologodskii, A.4    Kallenbach, N.R.5
  • 61
    • 0029919676 scopus 로고    scopus 로고
    • Ion pairs significantly stabilize coiled-coils in the absence of electrolyte
    • Yu Y., Monera O. D., Hodges R. S., Privalov P. L. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J. Mol. Biol. 255:1996;367-372.
    • (1996) J. Mol. Biol. , vol.255 , pp. 367-372
    • Yu, Y.1    Monera, O.D.2    Hodges, R.S.3    Privalov, P.L.4
  • 62
    • 0028036221 scopus 로고
    • Alpha helix capping in synthetic model peptides by reciprocal side-chain-main-chain interactions: Evidence for an N-terminal capping box
    • Zhou H. X., Lyu P. C., Wemmer D. E., Kallenbach N. R. Alpha helix capping in synthetic model peptides by reciprocal side-chain-main-chain interactions: Evidence for an N-terminal capping box. Proteins: Struct. Funct. Genet. 18:1994;1-7.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 1-7
    • Zhou, H.X.1    Lyu, P.C.2    Wemmer, D.E.3    Kallenbach, N.R.4
  • 63
    • 0028364239 scopus 로고
    • The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils
    • Zhou N. E., Kay C. M., Hodges R. S. The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils. J. Mol. Biol. 237:1994;500-512.
    • (1994) J. Mol. Biol. , vol.237 , pp. 500-512
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 64
    • 0027475082 scopus 로고
    • Packing and hydrophobicity effects on protein folding and stability: Effects of beta-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded alpha-helical coiled coils/leucine zippers
    • Zhu B. Y., Zhou N. E., Kay C. M., Hodges R. S. Packing and hydrophobicity effects on protein folding and stability: effects of beta-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded alpha-helical coiled coils/leucine zippers. Protein Sci. 2:1993;383-394.
    • (1993) Protein Sci. , vol.2 , pp. 383-394
    • Zhu, B.Y.1    Zhou, N.E.2    Kay, C.M.3    Hodges, R.S.4
  • 65
    • 0027980822 scopus 로고
    • Contribution to global protein stabilization of the N-capping box in human growth hormone
    • Zhukovsky E. A., Mulkerrin M. G., Presta L. G. Contribution to global protein stabilization of the N-capping box in human growth hormone. Biochemistry. 33:1994;9856-9864.
    • (1994) Biochemistry , vol.33 , pp. 9856-9864
    • Zhukovsky, E.A.1    Mulkerrin, M.G.2    Presta, L.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.