메뉴 건너뛰기




Volumn 11, Issue 3, 2015, Pages 221-228

Local and macroscopic electrostatic interactions in single α-helices

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA HELIX; ARTICLE; BIOINFORMATICS; CIRCULAR DICHROISM; CONTROLLED STUDY; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PEPTIDE SYNTHESIS; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; STATIC ELECTRICITY; ULTRACENTRIFUGATION; AMINO ACID SEQUENCE; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; MOLECULAR GENETICS; PROTEIN UNFOLDING;

EID: 84925533256     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1739     Document Type: Article
Times cited : (70)

References (57)
  • 1
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K.A. Dominant forces in protein folding. Biochemistry 29, 7133-7155 (1990).
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 2
    • 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, 205-211 (1951).
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 5
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of RNase-A
    • Bierzynski, A., Kim, P.S. & Baldwin, R.L. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase-A. Proc. Natl. Acad. Sci. USA 79, 2470-2474 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2470-2474
    • Bierzynski, A.1    Kim, P.S.2    Baldwin, R.L.3
  • 6
    • 0021281005 scopus 로고
    • A helix stop signal in the isolated S-peptide of ribonuclease-A
    • Kim, P.S. & Baldwin, R.L. A helix stop signal in the isolated S-peptide of ribonuclease-A. Nature 307, 329-334 (1984).
    • (1984) Nature , vol.307 , pp. 329-334
    • Kim, P.S.1    Baldwin, R.L.2
  • 7
    • 0023461350 scopus 로고
    • Helix stabilization by Glu-Lys+ salt bridges in short peptides of de novo design
    • Marqusee, S. & Baldwin, R.L. Helix stabilization by Glu-Lys+ salt bridges in short peptides of de novo design. Proc. Natl. Acad. Sci. USA 84, 8898-8902 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8898-8902
    • Marqusee, S.1    Baldwin, R.L.2
  • 8
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a-helices
    • Richardson, J.S. & Richardson, D.C. Amino acid preferences for specific locations at the ends of a-helices. Science 240, 1648-1652 (1988).
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 9
    • 0029020484 scopus 로고
    • N-and C-capping preferences for all 20 amino acids in a-helical peptides
    • Doig, A.J. & Baldwin, R.L. N-and C-capping preferences for all 20 amino acids in a-helical peptides. Protein Sci. 4, 1325-1336 (1995).
    • (1995) Protein Sci. , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 10
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace, C.N. & Scholtz, M.J. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 75, 422-427 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, M.J.2
  • 11
    • 0033582944 scopus 로고    scopus 로고
    • Side-chain structures in the first turn of the a-helix
    • Penel, S., Hughes, E. & Doig, A.J. Side-chain structures in the first turn of the a-helix. J. Mol. Biol. 287, 127-143 (1999).
    • (1999) J. Mol. Biol. , vol.287 , pp. 127-143
    • Penel, S.1    Hughes, E.2    Doig, A.J.3
  • 12
    • 23244461418 scopus 로고    scopus 로고
    • Anticooperativity in a Glu-Lys-Glu salt bridge triplet in an isolated a-helical peptide
    • Iqbalsyah, T.M. & Doig, A.J. Anticooperativity in a Glu-Lys-Glu salt bridge triplet in an isolated a-helical peptide. Biochemistry 44, 10449-10456 (2005).
    • (2005) Biochemistry , vol.44 , pp. 10449-10456
    • Iqbalsyah, T.M.1    Doig, A.J.2
  • 13
    • 0031764838 scopus 로고    scopus 로고
    • Surface salt bridges stabilize the GCN4 leucine zipper
    • Spek, E.J., Bui, A.H., Lu, M. & Kallenbach, N.R. Surface salt bridges stabilize the GCN4 leucine zipper. Protein Sci. 7, 2431-2437 (1998).
    • (1998) Protein Sci. , vol.7 , pp. 2431-2437
    • Spek, E.J.1    Bui, A.H.2    Lu, M.3    Kallenbach, N.R.4
  • 14
    • 0032556196 scopus 로고    scopus 로고
    • Stabilizing effect of a multiple salt bridge in a prenucleated peptide
    • Mayne, L. et al. Stabilizing effect of a multiple salt bridge in a prenucleated peptide. J. Am. Chem. Soc. 120, 10643-10645 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10643-10645
    • Mayne, L.1
  • 15
  • 16
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz, J.M., Qian, H., Robbins, V.H. & Baldwin, R.L. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry 32, 9668-9676 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 17
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for stabilization of a-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 a-helices. Nature 326, 563-567 (1987).
    • (1987) 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
  • 18
    • 0027524623 scopus 로고
    • Charged histidine affects a-helix stability at all positions in the helix by interacting with the backbone charges
    • Armstrong, K.M. & Baldwin, R.L. Charged histidine affects a-helix stability at all positions in the helix by interacting with the backbone charges. Proc. Natl. Acad. Sci. USA 90, 11337-11340 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11337-11340
    • Armstrong, K.M.1    Baldwin, R.L.2
  • 19
    • 0017292056 scopus 로고
    • The a-helix as an electric macro-dipole
    • Wada, A. The a-helix as an electric macro-dipole. Adv. Biophys. 1-63 (1976).
    • (1976) Adv. Biophys. , pp. 1-63
    • Wada, A.1
  • 20
    • 0017881332 scopus 로고
    • The a-helix dipole and the properties of proteins
    • Hol, W.G.J., van Duijnen, P.T. & Berendsen, H.J.C. The a-helix dipole and the properties of proteins. Nature 273, 443-446 (1978).
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 21
    • 0028350240 scopus 로고
    • An assessment of the effect of the helix dipole in protein structures
    • Chakrabarti, P. An assessment of the effect of the helix dipole in protein structures. Protein Eng. 7, 471-474 (1994).
    • (1994) Protein Eng , vol.7 , pp. 471-474
    • Chakrabarti, P.1
  • 22
    • 0025718955 scopus 로고
    • Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
    • Sun, D.P., Sauer, U., Nicholson, H. & Matthews, B.W. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 30, 7142-7153 (1991).
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Sun, D.P.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 23
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb, K.J. & Kim, P.S. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science 268, 436-439 (1995).
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 24
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled-coil stability, and specificity of dimerization
    • Lavigne, P., Sönnichsen, F.D., Kay, C.M. & Hodges, K.J. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science 271, 1136-1138 (1996).
    • (1996) Science , vol.271 , pp. 1136-1138
    • Lavigne, P.1    Sönnichsen, F.D.2    Kay, C.M.3    Hodges, K.J.4
  • 26
    • 0025800040 scopus 로고
    • A long helix from the central region of smooth muscle caldesmon
    • Wang, C.L. et al. A long helix from the central region of smooth muscle caldesmon. J. Biol. Chem. 266, 13958-13963 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 13958-13963
    • Wang, C.L.1
  • 27
  • 28
    • 63449140406 scopus 로고    scopus 로고
    • A FERM domain autoregulates Drosophila myosin 7a activity
    • Yang, Y. et al. A FERM domain autoregulates Drosophila myosin 7a activity. Proc. Natl. Acad. Sci. USA 106, 4189-4194 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4189-4194
    • Yang, Y.1
  • 29
    • 25844528995 scopus 로고    scopus 로고
    • The predicted coiled-coil domain of myosin 10 forms a novel elongated domain that lengthens the head
    • Knight, P.J. et al. The predicted coiled-coil domain of myosin 10 forms a novel elongated domain that lengthens the head. J. Biol. Chem. 280, 34702-34708 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 34702-34708
    • Knight, P.J.1
  • 30
    • 70349266063 scopus 로고    scopus 로고
    • When a predicted coiled coil is really a single a-helix, in myosins and other proteins
    • Peckham, M. & Knight, P.J. When a predicted coiled coil is really a single a-helix, in myosins and other proteins. Soft Matter 5, 2493-2503 (2009).
    • (2009) Soft Matter , vol.5 , pp. 2493-2503
    • Peckham, M.1    Knight, P.J.2
  • 32
    • 84857301203 scopus 로고    scopus 로고
    • Charged single alpha-helices in proteomes revealed by a consensus prediction approach
    • Gáspári, Z., Suveges, D., Perczel, A., Nyitray, L. & Toth, G. Charged single alpha-helices in proteomes revealed by a consensus prediction approach. Biochim. Biophys. Acta 1824, 637-646 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 637-646
    • Gáspári, Z.1    Suveges, D.2    Perczel, A.3    Nyitray, L.4    Toth, G.5
  • 33
    • 80053375422 scopus 로고    scopus 로고
    • Coiled coils and SAH domains in cytoskeletal molecular motors
    • Peckham, M. Coiled coils and SAH domains in cytoskeletal molecular motors. Biochem. Soc. Trans. 39, 1142-1148 (2011).
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1142-1148
    • Peckham, M.1
  • 35
    • 0026565486 scopus 로고
    • Energetic contribution of solvent-exposed ion-pairs to a-helix structure
    • Lyu, P.C.C., Gans, P.J. & Kallenbach, N.R. Energetic contribution of solvent-exposed ion-pairs to a-helix structure. J. Mol. Biol. 223, 343-350 (1992).
    • (1992) J. Mol. Biol. , vol.223 , pp. 343-350
    • Lyu, P.C.C.1    Gans, P.J.2    Kallenbach, N.R.3
  • 36
    • 0035106699 scopus 로고    scopus 로고
    • Effect of the N1 residue on the stability of the a-helix for all 20 amino acids
    • Cochran, D.A.E., Penel, S. & Doig, A.J. Effect of the N1 residue on the stability of the a-helix for all 20 amino acids. Protein Sci. 10, 463-470 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 463-470
    • Cochran, D.A.E.1    Penel, S.2    Doig, A.J.3
  • 37
    • 0034974668 scopus 로고    scopus 로고
    • Effect of the N2 residue on the stability of the a-helix for all 20 amino acids
    • Cochran, D.A.E. & Doig, A.J. Effect of the N2 residue on the stability of the a-helix for all 20 amino acids. Protein Sci. 10, 1305-1311 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 1305-1311
    • Cochran, D.A.E.1    Doig, A.J.2
  • 38
    • 0346733335 scopus 로고    scopus 로고
    • Effect of the N3 residue on the stability of the a-helix
    • Iqbalsyah, T.M. & Doig, A.J. Effect of the N3 residue on the stability of the a-helix. Protein Sci. 13, 32-39 (2004).
    • (2004) Protein Sci. , vol.13 , pp. 32-39
    • Iqbalsyah, T.M.1    Doig, A.J.2
  • 39
    • 0029166122 scopus 로고
    • Destabilization of a protein helix by electrostatic interactions
    • Walter, S., Hubner, B., Hahn, U. & Schmid, F.X. Destabilization of a protein helix by electrostatic interactions. J. Mol. Biol. 252, 133-143 (1995).
    • (1995) J. Mol. Biol. , vol.252 , pp. 133-143
    • Walter, S.1    Hubner, B.2    Hahn, U.3    Schmid, F.X.4
  • 40
    • 0025849701 scopus 로고
    • Calorimetric determination of the enthalpy change for the a-helix to coil transition of an alanine peptide in water
    • Scholtz, J.M. et al. Calorimetric determination of the enthalpy change for the a-helix to coil transition of an alanine peptide in water. Proc. Natl. Acad. Sci. USA 88, 2854-2858 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2854-2858
    • Scholtz, J.M.1
  • 41
    • 0032486233 scopus 로고    scopus 로고
    • Intrahelical side chain interactions in a-helices: Poor correlation between energetics and frequency
    • Fernández-Recio, J. & Sancho, J. Intrahelical side chain interactions in a-helices: poor correlation between energetics and frequency. FEBS Lett. 429, 99-103 (1998).
    • (1998) FEBS Lett. , vol.429 , pp. 99-103
    • Fernández-Recio, J.1    Sancho, J.2
  • 42
    • 78650141978 scopus 로고    scopus 로고
    • Amino acid pair-and triplet-wise groupings in the interior of a-helical segments in proteins
    • de Sousa, M.M. et al. Amino acid pair-and triplet-wise groupings in the interior of a-helical segments in proteins. J. Theor. Biol. 271, 136-144 (2011).
    • (2011) J. Theor. Biol. , vol.271 , pp. 136-144
    • De Sousa, M.M.1
  • 43
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H.M. et al. The Protein Data Bank. Nucleic Acids Res. 28, 235-242 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 44
    • 0028304962 scopus 로고
    • Satisfying hydrogen-bonding potential in proteins
    • McDonald, I.K. & Thornton, J.M. Satisfying hydrogen-bonding potential in proteins. J. Mol. Biol. 238, 777-793 (1994).
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 45
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of a-helices: Local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
    • Lacroix, E., Viguera, A.R. & Serrano, L. Elucidating the folding problem of a-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J. Mol. Biol. 284, 173-191 (1998).
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 46
    • 84855513111 scopus 로고    scopus 로고
    • Systematic control of protein interaction using a modular ER/K a-helix linker
    • Sivaramakrishnan, S. & Spudich, J.A. Systematic control of protein interaction using a modular ER/K a-helix linker. Proc. Natl. Acad. Sci. USA 108, 20467-20472 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20467-20472
    • Sivaramakrishnan, S.1    Spudich, J.A.2
  • 47
    • 76049109811 scopus 로고    scopus 로고
    • The SAH domain extends the functional length of the myosin lever
    • Baboolal, T.G. et al. The SAH domain extends the functional length of the myosin lever. Proc. Natl. Acad. Sci. USA 106, 22193-22198 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 22193-22198
    • Baboolal, T.G.1
  • 48
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz, J.M., Qian, H., York, E.J., Stewart, J.M. & Baldwin, R.L. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers 31, 1463-1470 (1991).
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 49
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers, J.K., Pace, C.N. & Scholtz, J.M. A direct comparison of helix propensity in proteins and peptides. Proc. Natl. Acad. Sci. USA 94, 2833-2837 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 50
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield, N.J. Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat. Protoc. 1, 2527-2535 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 51
    • 84898899006 scopus 로고    scopus 로고
    • A parametrically constrained optimization method for fitting sedimentation velocity experiments
    • Gorbet, G. et al. A parametrically constrained optimization method for fitting sedimentation velocity experiments. Biophys. J. 106, 1741-1750 (2014).
    • (2014) Biophys. J. , vol.106 , pp. 1741-1750
    • Gorbet, G.1
  • 52
    • 79954427635 scopus 로고    scopus 로고
    • Random coil chemical shift for intrinsically disordered proteins: Effects of temperature and pH
    • Kjaergaard, M., Brander, S. & Poulsen, F.M. Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH. J. Biomol. NMR 49, 139-149 (2011).
    • (2011) J. Biomol. NMR , vol.49 , pp. 139-149
    • Kjaergaard, M.1    Brander, S.2    Poulsen, F.M.3
  • 53
    • 80051704532 scopus 로고    scopus 로고
    • Sequence correction of random coil chemical shifts: Correlation between neighbor correction factors and changes in the Ramachandran distribution
    • Kjaergaard, M. & Poulsen, F.M. Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution. J. Biomol. NMR 50, 157-165 (2011).
    • (2011) J. Biomol. NMR , vol.50 , pp. 157-165
    • Kjaergaard, M.1    Poulsen, F.M.2
  • 54
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang, G. & Dunbrack, R.L. PISCES: a protein sequence culling server. Bioinformatics 19, 1589-1591 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack, R.L.2
  • 55
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. & Thornton, J.M. PROMOTIF - A program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 56
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.