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Volumn 75, Issue 4, 2009, Pages 911-918

Effect of pressure on helix-coil transition of an alanine-based peptide: An FTIR study

Author keywords

helix; CD spectra; Infrared spectra; Partial molar volume; Pressure induced folding

Indexed keywords

ALANINE; AMIDE; PEPTIDE;

EID: 66149171368     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22302     Document Type: Article
Times cited : (45)

References (32)
  • 1
    • 0001435569 scopus 로고
    • The coagulation of albumen by pressure
    • Bridgman PW. The coagulation of albumen by pressure. J Biol Chem 1914;19:511-512.
    • (1914) J Biol Chem , vol.19 , pp. 511-512
    • Bridgman, P.W.1
  • 2
    • 36849150819 scopus 로고
    • Thermodynamics of unfolding
    • Kauzmann W. Thermodynamics of unfolding. Nature 1987;325:763-764.
    • (1987) Nature , vol.325 , pp. 763-764
    • Kauzmann, W.1
  • 5
    • 0032536156 scopus 로고    scopus 로고
    • Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy
    • DOI 10.1006/jmbi.1997.1454
    • Panick G, Malessa R, Winter R, Rapp G, Frye KJ, Royer CA. Structural characterization of the pressure-denatured state and unfolding/ refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy. J Mol Biol 1998;275:389-402. (Pubitemid 28030012)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.2 , pp. 389-402
    • Panick, G.1    Malessa, R.2    Winter, R.3    Rapp, G.4    Frye, K.J.5    Royer, C.A.6
  • 6
    • 0029024519 scopus 로고
    • Pressure- and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy
    • Takeda N, Kato M, Taniguchi Y. Pressure- and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy. Biochemistry 1995;34:5980-5987.
    • (1995) Biochemistry , vol.34 , pp. 5980-5987
    • Takeda, N.1    Kato, M.2    Taniguchi, Y.3
  • 7
    • 0036231272 scopus 로고    scopus 로고
    • Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin
    • Meersman F, Smeller L, Heremans K. Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophys J 2002;82:2635-2644. (Pubitemid 34441301)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2635-2644
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 9
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee S, Robbins VH, Baldwin RL. Unusually stable helix formation in short alanine-based peptides. Proc Natl Acad Sci USA 1989;86:5286-5290.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 11
    • 0027119143 scopus 로고
    • Internal stark effect measurement of the electric field at the amino terminus of an alpha helix
    • Lockhart DJ, Kim PS. Internal stark effect measurement of the electric field at the amino terminus of an alpha helix. Science 1992;257:947-951.
    • (1992) Science , vol.257 , pp. 947-951
    • Lockhart, D.J.1    Kim, P.S.2
  • 13
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/ water mixtures back to water
    • DOI 10.1021/bi9707133
    • Luo P, Baldwin RL. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 1997;36:8413-8421. (Pubitemid 27297553)
    • (1997) Biochemistry , vol.36 , Issue.27 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 15
    • 0026254055 scopus 로고
    • Parameter of helix-coil transition theory for alanine-based peptides of varying chain length in water
    • Scholtz JM, Qian H, York EJ, Stewart JM, Baldwin RL. Parameter of helix-coil transition theory for alanine-based peptides of varying chain length in water. Biopolymers 1991;31:1463-1470.
    • (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
  • 16
    • 0028289435 scopus 로고
    • Determination of free energies of N-capping in α-helices by modification of the Lifson-Roig helix-coil theory to include N- And C-capping
    • Doig AJ, Chakrabartty A, Klingler TM, Baldwin RL. 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 1994;33:3396-3403. (Pubitemid 24112654)
    • (1994) Biochemistry , vol.33 , Issue.11 , pp. 3396-3403
    • Doig, A.J.1    Chakrabartty, A.2    Klingler, T.M.3    Baldwin, R.L.4
  • 18
    • 20444366970 scopus 로고    scopus 로고
    • Pressure-tuning FT-IR spectroscopic study on the helix-coil transition of Ala-rich oligopeptide in aqueous solution
    • DOI 10.1016/j.bbapap.2005.02.014, PII S1570963905000713
    • Takekiyo T, Shimizu A, Kato M, Taniguchi Y. Pressure-tuning spectroscopic study on the helix-coil transition of Ala-rich oligopeptide in aqueous solution. Biochim Biophys Acta 2005;1750:1-4. (Pubitemid 40797719)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1750 , Issue.1 , pp. 1-4
    • Takekiyo, T.1    Shimizu, A.2    Kato, M.3    Taniguchi, Y.4
  • 20
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S, Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Protein Chem 1986;38:181-364.
    • (1986) Adv Protein Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 21
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • DOI 10.1021/bi00053a001
    • Surewicz WK, Mantsch HH, Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry 1993;32:389-394. (Pubitemid 23034873)
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 22
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • DOI 10.1017/S0033583502003815
    • Barth A, Zscherp C. What vibrations tell us about proteins. Q Rev Biophys 2002;35:369-430. (Pubitemid 36207229)
    • (2002) Quarterly Reviews of Biophysics , vol.35 , Issue.4 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 23
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm BH, Bragg JK. Theory of the phase transition between helix and random coil in polypeptide chains. J Chem Phys 1959;31:526-535.
    • (1959) J Chem Phys , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2
  • 24
    • 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
    • DOI 10.1016/j.jmb.2005.08.053, PII S0022283605010077
    • Zagrovic B, Jayachandran G, Millett IS, Doniachc S, Pande VS. How large is an alpha-helix? Studies of the radii of gyration of helical peptides by small-angle X-ray scattering and molecular dynamics. J Mol Biol 2005;353:232-241. (Pubitemid 41356608)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.2 , pp. 232-241
    • Zagrovic, B.1    Jayachandran, G.2    Millett, I.S.3    Doniach, S.4    Pande, V.S.5
  • 25
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N, Fasman GD. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969;8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 27
    • 0037059026 scopus 로고    scopus 로고
    • Recent advances in helix-coil theory
    • DOI 10.1016/S0301-4622(02)00170-9, PII S0301462202001709
    • Doig AJ. Recent advances in helix-coil theory. Biophys Chem 2002;101-102:281-293. (Pubitemid 35462053)
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 281-293
    • Doig, A.J.1
  • 28
    • 0034285165 scopus 로고    scopus 로고
    • IR spectroscopy of isotope-labeled helical peptides: Probing the effect of N-acetylation on helix stability
    • DOI 10.1002/1097-0282(200009)54:3<180::AID-BIP40>3.0.CO;2-9
    • Decatur SM. Infrared spectroscopy of isotopically labeled helical peptides: probing the effects on N-acetylation on helix stability. Biopolymers 2000;54:180-185. (Pubitemid 30482318)
    • (2000) Biopolymers , vol.54 , Issue.3 , pp. 180-185
    • Decatur, S.M.1
  • 29
    • 11844262057 scopus 로고    scopus 로고
    • Spectroscopic evidence for backbone desolvation of helical peptides by 2,2,2-trifluoroethanol: An isotope-edited FTIR study
    • DOI 10.1021/bi0481444
    • Starzyk A, Barber-Armstrong W, Sridharan M,Decatur SM. Spectroscopic evidence for backbone desolvation of helical peptides by 2,2,2-trifluoroethanol: an isotope-edited FTIR study. Biochemistry 2005;44:369-376. (Pubitemid 40095739)
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 369-376
    • Starzyk, A.1    Barber-Armstrong, W.2    Sridharan, M.3    Decatur, S.M.4
  • 30
    • 0029064280 scopus 로고
    • FTIR spectroscopy of alanine-based peptides: Assignment of the amide I' modes for random coil and helix
    • Martinez G, Millhauser G. FTIR spectroscopy of alanine-based peptides: assignment of the amide I' modes for random coil and helix. J Struct Biol 1995;114:23-37.
    • (1995) J Struct Biol , vol.114 , pp. 23-37
    • Martinez, G.1    Millhauser, G.2
  • 32
    • 36449001245 scopus 로고
    • Model calculations on the amide-I infrared bands of globular proteins
    • Torii H, Tasumi M. Model calculations on the amide-I infrared bands of globular proteins. J Chem Phys 1992;96:3379-3387.
    • (1992) J Chem Phys , vol.96 , pp. 3379-3387
    • Torii, H.1    Tasumi, M.2


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