메뉴 건너뛰기




Volumn 7, Issue 2, 1998, Pages 383-388

Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1

Author keywords

Helical propensity; Peptide; Ribonuclease T1; TFE; Trifluoroethanol; helix

Indexed keywords

PEPTIDE; RIBONUCLEASE T1; TRIFLUOROETHANOL;

EID: 0031889226     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070219     Document Type: Article
Times cited : (65)

References (35)
  • 1
    • 0028951041 scopus 로고
    • Stabilization of helical domains in short peptides using hydrophobic interactions
    • Albert JS, Hamilton AD. 1995. Stabilization of helical domains in short peptides using hydrophobic interactions. Biochemistry 34:984-990.
    • (1995) Biochemistry , vol.34 , pp. 984-990
    • Albert, J.S.1    Hamilton, A.D.2
  • 3
    • 0030599012 scopus 로고    scopus 로고
    • Insight into a random coil conformation and an isolated helix: Structural and dynamical characterisation of the C-helix peptide from hen lysozyme
    • Bolin KA, Pitkeathly M, Miranker A, Smith LJ, Dobson CM. 1996. Insight into a random coil conformation and an isolated helix: Structural and dynamical characterisation of the C-helix peptide from hen lysozyme. J Mol Biol 267:443-453.
    • (1996) J Mol Biol , vol.267 , pp. 443-453
    • Bolin, K.A.1    Pitkeathly, M.2    Miranker, A.3    Smith, L.J.4    Dobson, C.M.5
  • 4
    • 0030567341 scopus 로고    scopus 로고
    • Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol
    • Cammers-Goodwin A, Allen TJ, Oslick SL, McClure KF, Lee JH, Kemp DS. 1996. Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J Am Chem Soc 118:3082-3090.
    • (1996) J Am Chem Soc , vol.118 , pp. 3082-3090
    • Cammers-Goodwin, A.1    Allen, T.J.2    Oslick, S.L.3    McClure, K.F.4    Lee, J.H.5    Kemp, D.S.6
  • 6
    • 0014939887 scopus 로고
    • The effect of aliphatic alcohols on the helix-coil transition of poly-L-ornithine and poly-L-glutamic acid
    • Conio G, Patrone E, Brighetti S. 1970. The effect of aliphatic alcohols on the helix-coil transition of poly-L-ornithine and poly-L-glutamic acid. J Biol Chem 245:3335-3340.
    • (1970) J Biol Chem , vol.245 , pp. 3335-3340
    • Conio, G.1    Patrone, E.2    Brighetti, S.3
  • 7
    • 0028178865 scopus 로고
    • α-Helix-forming propensities in peptides and proteins
    • Creamer TP, Rose GD. 1994. α-Helix-forming propensities in peptides and proteins. Proteins Struct Funct Genet 19:85-97.
    • (1994) Proteins Struct Funct Genet , vol.19 , pp. 85-97
    • Creamer, T.P.1    Rose, G.D.2
  • 8
    • 0024385337 scopus 로고
    • Folding of a peptide corresponding to the α-helix in bovine pancreatic trypsin inhibitor
    • Goodman EM, Kim PS. 1989. Folding of a peptide corresponding to the α-helix in bovine pancreatic trypsin inhibitor. Biochemistry 28:4343-4347.
    • (1989) Biochemistry , vol.28 , pp. 4343-4347
    • Goodman, E.M.1    Kim, P.S.2
  • 9
    • 0001833867 scopus 로고
    • Conformational aspects of polypeptides. VIII. Helical assignments via far ultraviolet absorption spectra and optical activity
    • Goodman M, Listowsky I, Masuda Y, Boardman F. 1963. Conformational aspects of polypeptides. VIII. Helical assignments via far ultraviolet absorption spectra and optical activity. Biopolymers 1:33-42.
    • (1963) Biopolymers , vol.1 , pp. 33-42
    • Goodman, M.1    Listowsky, I.2    Masuda, Y.3    Boardman, F.4
  • 10
    • 0029588554 scopus 로고
    • High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
    • Hamada D, Kuroda Y, Toshiki T, Goto Y. 1995. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J Mol Biol 254:737-746.
    • (1995) J Mol Biol , vol.254 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Toshiki, T.3    Goto, Y.4
  • 11
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensities from trifluoroethanol titration curves
    • Jasanoff A, Fersht AR. 1994. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 33:2126-2135.
    • (1994) Biochemistry , vol.33 , pp. 2126-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 13
    • 0028838504 scopus 로고
    • Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor
    • Kemmink J, Creighton TE. 1995. Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor. Biochemistry 34:12630-12635.
    • (1995) Biochemistry , vol.34 , pp. 12630-12635
    • Kemmink, J.1    Creighton, T.E.2
  • 14
    • 0000333671 scopus 로고
    • On the theory of helix-coil transitions in biopolymers
    • Lifson R, Roig A. 1961. On the theory of helix-coil transitions in biopolymers. J Chem Phys 34:1963-1974.
    • (1961) J Chem Phys , vol.34 , pp. 1963-1974
    • Lifson, R.1    Roig, A.2
  • 15
    • 33847801579 scopus 로고
    • Charge relay at the peptide bond. A proton magnetic resonance study of solvation effects on the amide electron density distribution
    • Llinas M, Klein MP. 1975. Charge relay at the peptide bond. A proton magnetic resonance study of solvation effects on the amide electron density distribution. J Am Chem Soc 97:4731-4737.
    • (1975) J Am Chem Soc , vol.97 , pp. 4731-4737
    • Llinas, M.1    Klein, M.P.2
  • 16
    • 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
    • Luc P, Baldwin RL. 1997. Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol:water mixtures back to water. Biochemistry 36:8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luc, P.1    Baldwin, R.L.2
  • 17
    • 0002682169 scopus 로고    scopus 로고
    • Local versus nonlocal interactions in protein folding and stability - An experimentalists point of view
    • Muñoz V, Serrano L. 1996. Local versus nonlocal interactions in protein folding and stability - An experimentalists point of view. Folding & Design 1:R71-R77.
    • (1996) Folding & Design , vol.1
    • Muñoz, V.1    Serrano, L.2
  • 18
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers JK, Pace CN, Scholtz JM. 1997a. A direct comparison of helix propensity in proteins and peptides. Proc Natl Acad Sci USA 94:2833-2837.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 19
    • 0030858237 scopus 로고    scopus 로고
    • Helix propensities are identical in proteins and peptides
    • Myers JK, Pace CN, Scholtz JM. 1997b. Helix propensities are identical in proteins and peptides. Biochemistry 36:10923-10929.
    • (1997) Biochemistry , vol.36 , pp. 10923-10929
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 20
    • 0030297677 scopus 로고    scopus 로고
    • The α-helix of ribonuclease T1 as an independent stability unit: Direct comparison of peptide and protein stability
    • Myers JK, Smith JS, Pace CN, Scholtz JM. 1996. The α-helix of ribonuclease T1 as an independent stability unit: Direct comparison of peptide and protein stability. J Mol Biol 263:390-395.
    • (1996) J Mol Biol , vol.263 , pp. 390-395
    • Myers, J.K.1    Smith, J.S.2    Pace, C.N.3    Scholtz, J.M.4
  • 21
    • 0022804939 scopus 로고
    • Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol
    • Nelson JW, Kallenbach NR. 1986. Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol. Proteins Struct Funct Genet 1:211-217.
    • (1986) Proteins Struct Funct Genet , vol.1 , pp. 211-217
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 22
    • 0024473893 scopus 로고
    • Persistence of the α-helix stop signal in the S-peptide in trifluoroethanol solutions
    • Nelson JW, Kallenhach NR. 1989. Persistence of the α-helix stop signal in the S-peptide in trifluoroethanol solutions. Biochemistry 28:5256-5261.
    • (1989) Biochemistry , vol.28 , pp. 5256-5261
    • Nelson, J.W.1    Kallenhach, N.R.2
  • 23
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental sludies of peptides and proteins
    • In press
    • Pace CN, Scholtz JM. 1998. A helix propensity scale based on experimental sludies of peptides and proteins. Biophysical J. In press.
    • (1998) Biophysical J.
    • Pace, C.N.1    Scholtz, J.M.2
  • 24
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 25
    • 0027675592 scopus 로고
    • Single-residue substitution in homopolypeptides: Perturbative helix-coil theory at a single site
    • Qian H. 1993. Single-residue substitution in homopolypeptides: Perturbative helix-coil theory at a single site. Biopolymers 33:1605-1616.
    • (1993) Biopolymers , vol.33 , pp. 1605-1616
    • Qian, H.1
  • 26
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl CA, Chakrahartty A, Baldwin RL. 1996. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci 5:2623-2637.
    • (1996) Protein Sci , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrahartty, A.2    Baldwin, R.L.3
  • 27
    • 0026568185 scopus 로고
    • Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation
    • Rohl CA, Scholtz JM, York EJ, Stewart JM, Baldwin RL. 1992. Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation. Biochemistry 57:1263-1269.
    • (1992) Biochemistry , vol.57 , pp. 1263-1269
    • Rohl, C.A.1    Scholtz, J.M.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 29
    • 0000323824 scopus 로고
    • α-Helix formation by peptides in water
    • Gutte B, ed. San Diego, California: Academic Press
    • Scholtz JM, Baldwin RL. 1995. α-Helix formation by peptides in water. In: Gutte B, ed. Peptides: Synthesis, structures, and applications. San Diego, California: Academic Press. pp 171-192.
    • (1995) Peptides: Synthesis, Structures, and Applications , pp. 171-192
    • Scholtz, J.M.1    Baldwin, R.L.2
  • 30
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sonnischen FD, Van Eyk JE, Hodges RS, Sykes BD. 1992. Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide. Biochemistry 31:8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sonnischen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 31
    • 0027006857 scopus 로고
    • Helix propagation in trifluoroethanol solutions
    • Storrs RW, Truckses D, Wemmer DE. 1992. Helix propagation in trifluoroethanol solutions. Biopolymers 52:1695-1702.
    • (1992) Biopolymers , vol.52 , pp. 1695-1702
    • Storrs, R.W.1    Truckses, D.2    Wemmer, D.E.3
  • 32
    • 0029166122 scopus 로고
    • Destabilization of a protein helix by electrostatic interactions
    • Walter S, Hubner B, Hahn U, Schmid FX. 1995. Destabilization of a protein helix by electrostatic interactions. J Mol Biol 252:133-143.
    • (1995) J Mol Biol , vol.252 , pp. 133-143
    • Walter, S.1    Hubner, B.2    Hahn, U.3    Schmid, F.X.4
  • 33
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites 1. Secondary structure formation by peptides corresponding to the G- and H- helices of myoglobin
    • Waltho JP, Feher VA, Merutka G, Dyson HJ, Wright PE. 1993. Peptide models of protein folding initiation sites 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry 52:6337-6347.
    • (1993) Biochemistry , vol.52 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Merutka, G.3    Dyson, H.J.4    Wright, P.E.5
  • 34
    • 0029865495 scopus 로고    scopus 로고
    • Analysis of thermodynamic determinants in helix propensities of nonpolar amino acids through a novel free energy calculation
    • Wang J, Purisma EO. 1996. Analysis of thermodynamic determinants in helix propensities of nonpolar amino acids through a novel free energy calculation. J Am Chem Soc 118:995-1001.
    • (1996) J Am Chem Soc , vol.118 , pp. 995-1001
    • Wang, J.1    Purisma, E.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.