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Volumn 1258, Issue , 2015, Pages 347-369

Insoluble protein assemblies characterized by fourier transform infrared spectroscopy

Author keywords

Amyloid; Fourier transform infrared spectroscopy; Hydrogel; Inclusion body; Microspectroscopy; Peptide scaffold; Protein aggregation; Secondary structures; Spectroscopy; sheet

Indexed keywords

AMINO ACID; AMYLOID; POLYPEPTIDE; PROTEIN; RECOMBINANT PROTEIN; SCAFFOLD PROTEIN; PEPTIDE;

EID: 84958657006     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2205-5_20     Document Type: Article
Times cited : (36)

References (65)
  • 1
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL (1998) Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des 3:R9–R23
    • (1998) Fold Des , vol.3 , pp. R9-R23
    • Fink, A.L.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333–366
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 84856873460 scopus 로고    scopus 로고
    • Proteins fi brils from a polymer physics perspective
    • Adamcik J, Mezzenga R (2012) Proteins fi brils from a polymer physics perspective. Macro molecules 45:1137–1150
    • (2012) Macro molecules , vol.45 , pp. 1137-1150
    • Adamcik, J.1    Mezzenga, R.2
  • 4
    • 84867457304 scopus 로고    scopus 로고
    • Amyloid inspired self-assembled peptide nanofi bers
    • Cinar G, Ceylan H, Urel M et al (2012) Amyloid inspired self-assembled peptide nanofi bers. Biomacromolecules 13:3377–3387
    • (2012) Biomacromolecules , vol.13 , pp. 3377-3387
    • Cinar, G.1    Ceylan, H.2    Urel, M.3
  • 8
    • 79959952063 scopus 로고    scopus 로고
    • Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology
    • Gatti-Lafranconi P, Natalello A, Ami D et al (2011) Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology. FEBS J 278:2408–2418
    • (2011) FEBS J , vol.278 , pp. 2408-2418
    • Gatti-lafranconi, P.1    Natalello, A.2    Ami, D.3
  • 9
    • 77951571256 scopus 로고    scopus 로고
    • Tunable geometry of bacterial inclusion bodies as substrate materials for tissue engineering
    • Garcia-Fruitos E, Seras-Franzoso J, Vazquez E et al (2010) Tunable geometry of bacterial inclusion bodies as substrate materials for tissue engineering. Nanotechnology 21:205101
    • (2010) Nanotechnology , vol.21 , pp. 205101
    • Garcia-fruitos, E.1    Seras-franzoso, J.2    Vazquez, E.3
  • 11
    • 26844569776 scopus 로고    scopus 로고
    • Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fl uorescent proteins
    • Garcia-Fruitos E, Gonzalez-Montalban N, Morell M et al (2005) Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fl uorescent proteins. Microb Cell Fact 4:27
    • (2005) Microb Cell Fact , vol.4 , pp. 27
    • Garcia-fruitos, E.1    Gonzalez-montalban, N.2    Morell, M.3
  • 12
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri S, Khurana R, Fink AL (1999) Fourier transform infrared spectroscopy in analysis of protein deposits. Methods Enzymol 309: 559–576
    • (1999) Methods Enzymol , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 13
    • 84865315486 scopus 로고    scopus 로고
    • Fourier transform infrared microspectroscopy of complex biological systems: From intact cells to whole organisms
    • Uversky VN, Dunker AK (eds), Methods and experimental tools. Methods in molecular biology. Humana, New York
    • Ami D, Natalello A, Doglia SM (2012) Fourier transform infrared microspectroscopy of complex biological systems: from intact cells to whole organisms. In: Uversky VN, Dunker AK (eds) Intrinsically disordered protein analysis: volume 1-895, Methods and experimental tools. Methods in molecular biology. Humana, New York, pp 85–100. doi: 10.1007/978-1-61779-927-3_7
    • (2012) Intrinsically disordered protein analysis , vol.1-895 , pp. 85
    • Ami, D.1    Natalello, A.2    Doglia, S.M.3
  • 14
    • 84865323237 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy of intrinsically disordered proteins: Measurement procedures and data analyses
    • Uversky VN, Dunker AK (eds), Methods and experimental tools. Methods in molecular biology, vol 895. Humana, New York
    • Natalello A, Ami D, Doglia S (2012) Fourier transform infrared spectroscopy of intrinsically disordered proteins: measurement procedures and data analyses. In: Uversky VN, Dunker AK (eds) Intrinsically disordered protein analysis: volume 1, Methods and experimental tools. Methods in molecular biology, vol 895. Humana, New York, pp 229–244. doi: 10.1007/978- 1-61779-927-3_16
    • (2012) Intrinsically disordered protein analysis , vol.1 , pp. 229-244
    • Natalello, A.1    Ami, D.2    Doglia, S.3
  • 15
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth A (2007) Infrared spectroscopy of proteins. Biochim Biophys Acta 1767: 1073–1101
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 16
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native beta-sheet proteins and amyloid fi brils
    • Zandomeneghi G, Krebs MRH, McCammon MG et al (2004) FTIR reveals structural differences between native beta-sheet proteins and amyloid fi brils. Protein Sci 13:3314–3321
    • (2004) Protein Sci , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3
  • 17
    • 12844274977 scopus 로고    scopus 로고
    • Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy
    • Natalello A, Ami D, Brocca S et al (2005) Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy. Biochem J 385:511–517
    • (2005) Biochem J , vol.385 , pp. 511-517
    • Natalello, A.1    Ami, D.2    Brocca, S.3
  • 18
    • 33846243823 scopus 로고    scopus 로고
    • Role of fl avin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA
    • Natalello A, Doglia SM, Carey J et al (2007) Role of fl avin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA. Biochemistry 46:543–553
    • (2007) Biochemistry , vol.46 , pp. 543-553
    • Natalello, A.1    Doglia, S.M.2    Carey, J.3
  • 19
    • 79954618669 scopus 로고    scopus 로고
    • A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation
    • Natalello A, Frana AM, Relini A et al (2011) A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation. PLoS One 6:e18789
    • (2011) PLoS One , vol.6 , pp. 18789
    • Natalello, A.1    Frana, A.M.2    Relini, A.3
  • 20
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total refl ection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh E, Raussens V, Ruysschaert JM (1999) Attenuated total refl ection infrared spectroscopy of proteins and lipids in biological membranes. Biochim Biophys Acta 1422:105–185
    • (1999) Biochim Biophys Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.M.3
  • 21
    • 41049088527 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies
    • Doglia SM, Ami D, Natalello A et al (2008) Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies. Biotechnol J 3:193–201
    • (2008) Biotechnol J , vol.3 , pp. 193-201
    • Doglia, S.M.1    Ami, D.2    Natalello, A.3
  • 22
    • 0032078387 scopus 로고    scopus 로고
    • Application of infrared spectroscopy to development of stable lyophilized protein formulations
    • Carpenter JF, Prestrelski SJ, Dong A (1998) Application of infrared spectroscopy to development of stable lyophilized protein formulations. Eur J Pharm Biopharm 45:231–238
    • (1998) Eur J Pharm Biopharm , vol.45 , pp. 231-238
    • Carpenter, J.F.1    Prestrelski, S.J.2    Dong, A.3
  • 23
    • 84859416802 scopus 로고    scopus 로고
    • Structure, stability, and aggregation of β-2 microglobulin mutants: Insights from a Fourier transform infrared study in solution and in the crystalline state
    • Ami D, Ricagno S, Bolognesi M et al (2012) Structure, stability, and aggregation of β-2 microglobulin mutants: insights from a Fourier transform infrared study in solution and in the crystalline state. Biophys J 102:1676–1684
    • (2012) Biophys J , vol.102 , pp. 1676-1684
    • Ami, D.1    Ricagno, S.2    Bolognesi, M.3
  • 24
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A, Zscherp C (2002) What vibrations tell us about proteins. Q Rev Biophys 35:369–430
    • (2002) Q Rev Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 25
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo JLR, Goni FM (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog Biophys Mol Biol 72:367–405
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 26
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm LK, Tatulian SA (1997) Infrared spectroscopy of proteins and peptides in lipid bilayers. Q Rev Biophys 30:365–429
    • (1997) Q Rev Biophys , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 27
    • 79952937011 scopus 로고    scopus 로고
    • BMHP1-derived self-assembling peptides: Hierarchically assembled structures with self- healing propensity and potential for tissue engineering applications
    • Gelain F, Silva D, Caprini A et al (2011) BMHP1-derived self-assembling peptides: hierarchically assembled structures with self- healing propensity and potential for tissue engineering applications. ACS Nano 5:1845–1859
    • (2011) ACS Nano , vol.5 , pp. 1845-1859
    • Gelain, F.1    Silva, D.2    Caprini, A.3
  • 28
    • 84871737801 scopus 로고    scopus 로고
    • Synthesis and characterization of designed BMHP1- derived self-assembling peptides for tissue engineering applications
    • Silva D, Natalello A, Sanii B et al (2013) Synthesis and characterization of designed BMHP1- derived self-assembling peptides for tissue engineering applications. Nanoscale 5:704–718
    • (2013) Nanoscale , vol.5 , pp. 704-718
    • Silva, D.1    Natalello, A.2    Sanii, B.3
  • 29
    • 84871310867 scopus 로고    scopus 로고
    • The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli
    • Invernizzi G, Aprile FA, Natalello A et al (2012) The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli. PLoS One 7:e51890
    • (2012) PLoS One , vol.7 , pp. 51890
    • Invernizzi, G.1    Aprile, F.A.2    Natalello, A.3
  • 30
    • 84860660444 scopus 로고    scopus 로고
    • Toward understanding Machado–Joseph disease
    • Costa MC, Paulson HL (2012) Toward understanding Machado–Joseph disease. Prog Neurobiol 97:239–257
    • (2012) Prog Neurobiol , vol.97 , pp. 239-257
    • Costa, M.C.1    Paulson, H.L.2
  • 31
    • 0031070340 scopus 로고    scopus 로고
    • Infrared spectroscopy in aqueous solution: Diffi culties and accuracy of water subtraction
    • Rahmelow K, Hubner W (1997) Infrared spectroscopy in aqueous solution: diffi culties and accuracy of water subtraction. Appl Spectrosc 51:160–170
    • (1997) Appl Spectrosc , vol.51 , pp. 160-170
    • Rahmelow, K.1    Hubner, W.2
  • 32
    • 0031150139 scopus 로고    scopus 로고
    • Water (H 2 O and D 2 O) molar absorptivity in the 1000–4000 cm -1 range and quantitative infrared spectroscopy of aqueous solutions
    • Venyaminov SY, Prendergast FG (1997) Water (H 2 O and D 2 O) molar absorptivity in the 1000–4000 cm -1 range and quantitative infrared spectroscopy of aqueous solutions. Anal Biochem 248:234–245
    • (1997) Anal Biochem , vol.248 , pp. 234-245
    • Venyaminov, S.Y.1    Prendergast, F.G.2
  • 33
    • 0025357111 scopus 로고
    • Protein secondary structures in water from 2nd-derivative amide-I infrared-spectra
    • Dong A, Huang P, Caughey WS (1990) Protein secondary structures in water from 2nd-derivative amide-I infrared-spectra. Biochemistry 29:3303–3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 34
    • 48749090708 scopus 로고    scopus 로고
    • Conformational plasticity of the Gerstmann-Straussler-Scheinker disease peptide as indicated by its multiple aggregation pathways
    • Natalello A, Prokorov VV, Tagliavini F et al (2008) Conformational plasticity of the Gerstmann-Straussler-Scheinker disease peptide as indicated by its multiple aggregation pathways. J Mol Biol 381:1349–1361
    • (2008) J Mol Biol , vol.381 , pp. 1349-1361
    • Natalello, A.1    Prokorov, V.V.2    Tagliavini, F.3
  • 35
    • 84873744026 scopus 로고    scopus 로고
    • Why and how protein aggregation has to be studied in vivo
    • Ami D, Natalello A, Lotti M et al (2013) Why and how protein aggregation has to be studied in vivo. Microb Cell Fact 12:17
    • (2013) Microb Cell Fact , vol.12 , pp. 17
    • Ami, D.1    Natalello, A.2    Lotti, M.3
  • 36
    • 0029839357 scopus 로고    scopus 로고
    • In situ characterization of beta-amyloid in Alzheimer’s diseased tissue by synchrotron Fourier transform infrared microspectroscopy
    • Choo LP, Wetzel DL, Halliday WC et al (1996) In situ characterization of beta-amyloid in Alzheimer’s diseased tissue by synchrotron Fourier transform infrared microspectroscopy. Biophys J 71:1672–1679
    • (1996) Biophys J , vol.71 , pp. 1672-1679
    • Choo, L.P.1    Wetzel, D.L.2    Halliday, W.C.3
  • 37
    • 78650104379 scopus 로고    scopus 로고
    • Tetracycline and its analogues protect Caenorhabditis elegans from beta amyloidinduced toxicity by targeting oligomers
    • Diomede L, Cassata G, Fiordaliso F et al (2010) Tetracycline and its analogues protect Caenorhabditis elegans from beta amyloidinduced toxicity by targeting oligomers. Neurobiol Dis 40:424–431
    • (2010) Neurobiol Dis , vol.40 , pp. 424-431
    • Diomede, L.1    Cassata, G.2    Fiordaliso, F.3
  • 38
    • 0344395589 scopus 로고    scopus 로고
    • FT-IR study of heterologous protein expression in recombinant Escherichia coli strains
    • Ami D, Bonecchi L, Cali S et al (2003) FT-IR study of heterologous protein expression in recombinant Escherichia coli strains. Biochim Biophys Acta 1624:6–10
    • (2003) Biochim Biophys Acta , vol.1624 , pp. 6-10
    • Ami, D.1    Bonecchi, L.2    Cali, S.3
  • 39
    • 20444363444 scopus 로고    scopus 로고
    • Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    • Ami D, Natalello A, Gatti-Lafranconi P et al (2005) Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Lett 579:3433–3436
    • (2005) FEBS Lett , vol.579 , pp. 3433-3436
    • Ami, D.1    Natalello, A.2    Gatti-lafranconi, P.3
  • 40
    • 33646589053 scopus 로고    scopus 로고
    • Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy
    • Ami D, Natalello A, Taylor G et al (2006) Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy. Biochim Biophys Acta 1764:793–799
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 793-799
    • Ami, D.1    Natalello, A.2    Taylor, G.3
  • 42
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier-transform infrared-spectroscopy of enzymes
    • Susi H, Byler DM (1986) Resolution-enhanced Fourier-transform infrared-spectroscopy of enzymes. Methods Enzymol 130:290–311
    • (1986) Methods Enzymol , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 43
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared- spectroscopy
    • Arrondo JLR, Muga A, Castresana J et al (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared- spectroscopy. Prog Biophys Mol Biol 59:23–25
    • (1993) Prog Biophys Mol Biol , vol.59 , pp. 23-25
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3
  • 44
    • 0000337013 scopus 로고
    • Fourier self-deconvolution – a method for resolving intrinsically overlapped bands
    • Kauppinen JK, Moffatt DJ, Mantsch HH et al (1981) Fourier self-deconvolution – a method for resolving intrinsically overlapped bands. Appl Spectrosc 35:271–276
    • (1981) Appl Spectrosc , vol.35 , pp. 271-276
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3
  • 45
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures
    • Goormaghtigh E, Cabiaux V, Ruysschaert JM (1994) Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures. Sub-cell Biochem 23:405–450
    • (1994) Sub-cell Biochem , vol.23 , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 46
    • 0034076545 scopus 로고    scopus 로고
    • Do parallel betahelix proteins have a unique Fourier transform infrared spectrum?
    • Khurana R, Fink AL (2000) Do parallel betahelix proteins have a unique Fourier transform infrared spectrum? Biophys J 78:994–1000
    • (2000) Biophys J , vol.78 , pp. 994-1000
    • Khurana, R.1    Fink, A.L.2
  • 47
    • 0023442501 scopus 로고
    • Fourier-transform infrared study of proteins with parallel betachains
    • Susi H, Byler DM (1987) Fourier-transform infrared study of proteins with parallel betachains. Arch Biochem Biophys 258:465–469
    • (1987) Arch Biochem Biophys , vol.258 , pp. 465-469
    • Susi, H.1    Byler, D.M.2
  • 48
    • 0032978519 scopus 로고    scopus 로고
    • The nucleation of monomeric parallel beta-sheet-like structures and their selfassembly in aqueous solution
    • Chitnumsub P, Fiori WR, Lashuel HA et al (1999) The nucleation of monomeric parallel beta-sheet-like structures and their selfassembly in aqueous solution. Bioorg Med Chem 7:39–59
    • (1999) Bioorg Med Chem , vol.7 , pp. 39-59
    • Chitnumsub, P.1    Fiori, W.R.2    Lashuel, H.A.3
  • 49
    • 0032477320 scopus 로고    scopus 로고
    • Regulation of b-sheet structures within amyloid- like b-sheet assemblage from tripeptide derivatives
    • Yamada N, Ariga K, Naito M et al (1998) Regulation of b-sheet structures within amyloid- like b-sheet assemblage from tripeptide derivatives. J Am Chem Soc 120: 12192–12199
    • (1998) J Am Chem Soc , vol.120 , pp. 12192-12199
    • Yamada, N.1    Ariga, K.2    Naito, M.3
  • 50
    • 69249239132 scopus 로고    scopus 로고
    • Antiparallel β-sheet: A signature structure of the oligomeric amyloid β-peptide
    • Cerf E, Sarroukh R, Tamamizu-Kato S et al (2009) Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide. Biochem J 421:415–423
    • (2009) Biochem J , vol.421 , pp. 415-423
    • Cerf, E.1    Sarroukh, R.2    Tamamizu-kato, S.3
  • 51
    • 84884297163 scopus 로고    scopus 로고
    • ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins
    • Sarroukh R, Goormaghtigh E, Ruysschaert JM et al (2013) ATR-FTIR: a “rejuvenated” tool to investigate amyloid proteins. Biochim Biophys Acta 1828:2328–2338
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 2328-2338
    • Sarroukh, R.1    Goormaghtigh, E.2    Ruysschaert, J.M.3
  • 52
    • 0001443463 scopus 로고    scopus 로고
    • Effects of hydration on the structure, vibrational wavenumbers, vibrational force fi eld and resonance raman intensities of N-methylacetamide
    • Torii H, Tatsumi T, Tasumi M (1998) Effects of hydration on the structure, vibrational wavenumbers, vibrational force fi eld and resonance raman intensities of N-methylacetamide. J Raman Spectrosc 29:537–546
    • (1998) J Raman Spectrosc , vol.29 , pp. 537-546
    • Torii, H.1    Tatsumi, T.2    Tasumi, M.3
  • 53
    • 84875212796 scopus 로고    scopus 로고
    • Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates
    • Natalello A, Mattoo RUH, Priya S et al (2013) Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates. J Mol Biol 425:1158–1171
    • (2013) J Mol Biol , vol.425 , pp. 1158-1171
    • Natalello, A.1    Mattoo, R.U.H.2    Priya, S.3
  • 54
    • 0035811052 scopus 로고    scopus 로고
    • Lifetimes of intermediates in the betasheet to alpha-helix transition of betalactoglobulin by using a diffusional IR mixer
    • Kauffmann E, Darnton NC, Austin RH et al (2001) Lifetimes of intermediates in the betasheet to alpha-helix transition of betalactoglobulin by using a diffusional IR mixer. Proc Natl Acad Sci U S A 98:6646–6649
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6646-6649
    • Kauffmann, E.1    Darnton, N.C.2    Austin, R.H.3
  • 55
    • 0031584275 scopus 로고    scopus 로고
    • Structural changes in a secretory phospholipase A(2) induced by membrane binding: A clue to interfacial activation?
    • Tatulian SA, Biltonen RL, Tamm LK (1997) Structural changes in a secretory phospholipase A(2) induced by membrane binding: a clue to interfacial activation? J Mol Biol 268:809–815
    • (1997) J Mol Biol , vol.268 , pp. 809-815
    • Tatulian, S.A.1    Biltonen, R.L.2    Tamm, L.K.3
  • 56
    • 0037370999 scopus 로고    scopus 로고
    • The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR
    • Walsh STR, Cheng RP, Wright WW et al (2003) The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR. Protein Sci 12:520–531
    • (2003) Protein Sci , vol.12 , pp. 520-531
    • Walsh, S.T.R.1    Cheng, R.P.2    Wright, W.W.3
  • 57
    • 0029064280 scopus 로고
    • Ftir spectroscopy of alanine-based peptides – assignment of the amide I' modes for random coil and helix
    • Martinez G, Millhauser G (1995) Ftir spectroscopy of alanine-based peptides – assignment of the amide I' modes for random coil and helix. J Struct Biol 114:23–27
    • (1995) J Struct Biol , vol.114 , pp. 23-27
    • Martinez, G.1    Millhauser, G.2
  • 58
    • 67749129325 scopus 로고    scopus 로고
    • Alpha-helix stabilization within a peptide dendrimer
    • Javor S, Natalello A, Doglia SM et al (2008) Alpha-helix stabilization within a peptide dendrimer. J Am Chem Soc 130:17248–17249
    • (2008) J Am Chem Soc , vol.130 , pp. 17248-17249
    • Javor, S.1    Natalello, A.2    Doglia, S.M.3
  • 59
    • 25444523218 scopus 로고    scopus 로고
    • DNAinduced secondary structure of the carboxylterminal domain of histone H1
    • Roque A, Iloro I, Ponte I et al (2005) DNAinduced secondary structure of the carboxylterminal domain of histone H1. J Biol Chem 280:32141–32147
    • (2005) J Biol Chem , vol.280 , pp. 32141-32147
    • Roque, A.1    Iloro, I.2    Ponte, I.3
  • 60
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth A (2000) The infrared absorption of amino acid side chains. Prog Biophys Mol Biol 74:141–173
    • (2000) Prog Biophys Mol Biol , vol.74 , pp. 141-173
    • Barth, A.1
  • 61
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris PI, Severcan F (1999) FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. J Mol Catal B: Enzym 7:207–221
    • (1999) J Mol Catal B: Enzym , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 62
    • 0035997270 scopus 로고    scopus 로고
    • Automatic amide I frequency selection for rapid quantifi cation of protein secondary structure from Fourier transform infrared spectra of proteins
    • Hering JA, Innocent PR, Haris PI (2002) Automatic amide I frequency selection for rapid quantifi cation of protein secondary structure from Fourier transform infrared spectra of proteins. Proteomics 2:839–849
    • (2002) Proteomics , vol.2 , pp. 839-849
    • Hering, J.A.1    Innocent, P.R.2    Haris, P.I.3
  • 63
    • 0035903114 scopus 로고    scopus 로고
    • Induction of secondary structure in a COOH- terminal peptide of histone H1 by interaction with the DNA
    • Vila R, Ponte I, Collado M et al (2001) Induction of secondary structure in a COOH- terminal peptide of histone H1 by interaction with the DNA. J Biol Chem 276:30898–30903
    • (2001) J Biol Chem , vol.276 , pp. 30898-30903
    • Vila, R.1    Ponte, I.2    Collado, M.3
  • 64
    • 0342862068 scopus 로고
    • Solvent deuterium isotope effects on acid–base equilibria
    • Salomaa P, Schaleger LL, Long FA (1964) Solvent deuterium isotope effects on acid–base equilibria. J Am Chem Soc 86:1–7
    • (1964) J Am Chem Soc , vol.86 , pp. 1-7
    • Salomaa, P.1    Schaleger, L.L.2    Long, F.A.3
  • 65
    • 0030249365 scopus 로고    scopus 로고
    • Differences in conformational dynamics of ribonucleases A and S as observed by infrared spectroscopy and hydrogen-deuterium exchange
    • Dong AC, Hyslop RM, Pringle DL (1996) Differences in conformational dynamics of ribonucleases A and S as observed by infrared spectroscopy and hydrogen-deuterium exchange. Arch Biochem Biophys 333:275–281
    • (1996) Arch Biochem Biophys , vol.333 , pp. 275-281
    • Dong, A.C.1    Hyslop, R.M.2    Pringle, D.L.3


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