메뉴 건너뛰기




Volumn 137, Issue 1, 2008, Pages 24-27

Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)10

Author keywords

Amide bands; Collagen; Proline puckering; Raman crystallography

Indexed keywords

AMIDE; COLLAGEN; PEPTIDE; PROLINE; PYRROLIDINE DERIVATIVE;

EID: 48849089986     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.06.008     Document Type: Article
Times cited : (10)

References (31)
  • 3
    • 0035045552 scopus 로고    scopus 로고
    • Structural bases of collagen stabilization induced by proline hydroxylation
    • Vitagliano L., Berisio R., Mazzarella L., and Zagari A. Structural bases of collagen stabilization induced by proline hydroxylation. Biopolymers 58 (2001) 459-464
    • (2001) Biopolymers , vol.58 , pp. 459-464
    • Vitagliano, L.1    Berisio, R.2    Mazzarella, L.3    Zagari, A.4
  • 6
    • 9144246166 scopus 로고    scopus 로고
    • Crystal structures of collagen model peptides with Pro-Hyp-Gly repeating sequence at 1.26 Ǻ resolution: implications for proline ring puckering
    • Okuyama K., Hongo C., Fukushima R., Wu G., Narita H., Noguchi K., Tanaka Y., and Nishino N. Crystal structures of collagen model peptides with Pro-Hyp-Gly repeating sequence at 1.26 Ǻ resolution: implications for proline ring puckering. Biopolymers 76 (2005) 367-377
    • (2005) Biopolymers , vol.76 , pp. 367-377
    • Okuyama, K.1    Hongo, C.2    Fukushima, R.3    Wu, G.4    Narita, H.5    Noguchi, K.6    Tanaka, Y.7    Nishino, N.8
  • 7
    • 20144385152 scopus 로고    scopus 로고
    • 9 at 1.55 Ǻ resolution shows up-puckering of the proline ring in the Xaa position
    • 9 at 1.55 Ǻ resolution shows up-puckering of the proline ring in the Xaa position. J. Biol. Chem. 280 (2005) 20397-20403
    • (2005) J. Biol. Chem. , vol.280 , pp. 20397-20403
    • Schumacher, M.1    Mizuno, K.2    Barchinger, H.3
  • 8
    • 0025290183 scopus 로고
    • Structural studies of bean pod mottle virus, capsid, and RNA in crystal and solution states by laser Raman spectroscopy
    • 501
    • Tiansheng L., Zhongguo C., Johnson J.E., and Thomas G.J.J. Structural studies of bean pod mottle virus, capsid, and RNA in crystal and solution states by laser Raman spectroscopy. Biochemistry 29 (1990) 508-5026 501
    • (1990) Biochemistry , vol.29 , pp. 508-5026
    • Tiansheng, L.1    Zhongguo, C.2    Johnson, J.E.3    Thomas, G.J.J.4
  • 9
    • 3142658015 scopus 로고    scopus 로고
    • Following ligand binding and ligand reactions in proteins via Raman crystallography
    • Carey P.R., and Dong J. Following ligand binding and ligand reactions in proteins via Raman crystallography. Biochemistry 43 (2004) 8885-8893
    • (2004) Biochemistry , vol.43 , pp. 8885-8893
    • Carey, P.R.1    Dong, J.2
  • 10
    • 38549131861 scopus 로고    scopus 로고
    • A novel method for detection of seleno-methionine incorporation in protein crystals via Raman microscopy
    • Vergara A., Merlino A., Pizzo E., D'Alessio G., and Mazzarella L. A novel method for detection of seleno-methionine incorporation in protein crystals via Raman microscopy. Acta Cryst. D: Biol. Cryst. D64 (2008) 167-171
    • (2008) Acta Cryst. D: Biol. Cryst. , vol.D64 , pp. 167-171
    • Vergara, A.1    Merlino, A.2    Pizzo, E.3    D'Alessio, G.4    Mazzarella, L.5
  • 11
    • 0032986173 scopus 로고    scopus 로고
    • Raman spectroscopy of protein and nucleic acid assemblies
    • Thomas G.J.J. Raman spectroscopy of protein and nucleic acid assemblies. Annu. Rev. Biophys. Biomol. Struct. 28 (1999) 1-27
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 1-27
    • Thomas, G.J.J.1
  • 12
  • 13
    • 47849092863 scopus 로고    scopus 로고
    • Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase
    • Merlino A., Verde C., di Prisco G., Mazzarella L., and Vergara A. Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase. Spectroscopy 22 (2008) 143-152
    • (2008) Spectroscopy , vol.22 , pp. 143-152
    • Merlino, A.1    Verde, C.2    di Prisco, G.3    Mazzarella, L.4    Vergara, A.5
  • 14
    • 36048991521 scopus 로고    scopus 로고
    • Advances in spectroscopic methods for biological crystals. 2. Raman spectroscopy
    • Carpentier P., Royant A., Ohana J., and Bourgeois D. Advances in spectroscopic methods for biological crystals. 2. Raman spectroscopy. J. Appl. Cryst. 40 (2007) 1113-1122
    • (2007) J. Appl. Cryst. , vol.40 , pp. 1113-1122
    • Carpentier, P.1    Royant, A.2    Ohana, J.3    Bourgeois, D.4
  • 15
    • 0344305773 scopus 로고    scopus 로고
    • The structure of tri-proline in water probed by polarized Raman, Fourier Transform Infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy
    • Schweitzer-Stenner R., Eker F., Perez A., Griebenow K., Cao X., and Nafie L.A. The structure of tri-proline in water probed by polarized Raman, Fourier Transform Infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy. Biopolymers 71 (2003) 558-568
    • (2003) Biopolymers , vol.71 , pp. 558-568
    • Schweitzer-Stenner, R.1    Eker, F.2    Perez, A.3    Griebenow, K.4    Cao, X.5    Nafie, L.A.6
  • 16
    • 3042750640 scopus 로고    scopus 로고
    • Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution
    • Eker F., Griebenow K., Cao X., Nafie L., and Schweitzer-Stenner R. Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution. Proc. Natl. Acad. Sci. US 101 (2004) 10054-10059
    • (2004) Proc. Natl. Acad. Sci. US , vol.101 , pp. 10054-10059
    • Eker, F.1    Griebenow, K.2    Cao, X.3    Nafie, L.4    Schweitzer-Stenner, R.5
  • 17
    • 2642567722 scopus 로고    scopus 로고
    • Ab1-28 fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution
    • Eker F., Griebenow G., and Schweitzer-Stenner R. Ab1-28 fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution. Biochemistry 43 (2004) 6893-6898
    • (2004) Biochemistry , vol.43 , pp. 6893-6898
    • Eker, F.1    Griebenow, G.2    Schweitzer-Stenner, R.3
  • 18
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio B., and Tamburro A.M. Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions. Chirality 14 (2002) 782-792
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 19
    • 19744362700 scopus 로고    scopus 로고
    • UV Resonance Raman determination of polyproline II, extended 2.51-helix, and β-sheet ψ angle energy landscape in poly-l-lysine and poly-l-glutamic acid
    • Mikhonin A.V., Myshakina N.S., Bykov S.V., and Asher S.A. UV Resonance Raman determination of polyproline II, extended 2.51-helix, and β-sheet ψ angle energy landscape in poly-l-lysine and poly-l-glutamic acid. J. Am. Chem. Soc. 127 (2005) 7712-7720
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7712-7720
    • Mikhonin, A.V.1    Myshakina, N.S.2    Bykov, S.V.3    Asher, S.A.4
  • 20
    • 0001934802 scopus 로고    scopus 로고
    • Ab initio molecular orbital study of the amide I vibrational interactions between the peptide groups in di- and tripeptides and considerations on the conformation of the extended helix
    • Torii H., and Tasumi M. Ab initio molecular orbital study of the amide I vibrational interactions between the peptide groups in di- and tripeptides and considerations on the conformation of the extended helix. J. Raman Spectrosc. 29 (1998) 81-86
    • (1998) J. Raman Spectrosc. , vol.29 , pp. 81-86
    • Torii, H.1    Tasumi, M.2
  • 21
    • 3142754280 scopus 로고    scopus 로고
    • UV Raman demonstrates that α-helix polyalanine peptides melt to polyproline II conformations
    • Asher S.A., Mikhonin A.V., and Bykov S.V. UV Raman demonstrates that α-helix polyalanine peptides melt to polyproline II conformations. J. Am. Chem. Soc. 126 (2004) 8433-8440
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8433-8440
    • Asher, S.A.1    Mikhonin, A.V.2    Bykov, S.V.3
  • 22
    • 32544446167 scopus 로고    scopus 로고
    • Peptide secondary structure folding reaction coordinate: correlation between UV Raman amide III frequency, ψ Ramachandran angle, and hydrogen bonding
    • Mikhonin A.V., Bykov S.V., Myshakina N.S., and Asher S.A. Peptide secondary structure folding reaction coordinate: correlation between UV Raman amide III frequency, ψ Ramachandran angle, and hydrogen bonding. J. Phys. Chem. B 110 (2006) 1928-1943
    • (2006) J. Phys. Chem. B , vol.110 , pp. 1928-1943
    • Mikhonin, A.V.1    Bykov, S.V.2    Myshakina, N.S.3    Asher, S.A.4
  • 23
    • 0036795651 scopus 로고    scopus 로고
    • Granada Crystallisation Box: a new device for protein crystallisation by counter-diffusion techniques.
    • Garcia-Ruíz J., Gonzalez-Ramirez L., Gavira J., and Otálora F. Granada Crystallisation Box: a new device for protein crystallisation by counter-diffusion techniques. Acta Cryst. D: Biol. Cryst. 58 (2002) 1638-1642
    • (2002) Acta Cryst. D: Biol. Cryst. , vol.58 , pp. 1638-1642
    • Garcia-Ruíz, J.1    Gonzalez-Ramirez, L.2    Gavira, J.3    Otálora, F.4
  • 24
    • 0035965724 scopus 로고    scopus 로고
    • Dihedral ψ angle dependence of the amide III vibration: a uniquely sensitive UV resonance Raman secondary structural probe
    • Asher S.A., Ianoul A., Mix G., Boyden M.N., Karnoup A., Diem M., and Schweitzer-Stenner R. Dihedral ψ angle dependence of the amide III vibration: a uniquely sensitive UV resonance Raman secondary structural probe. J. Am. Chem. Soc. 123 (2001) 11775-11781
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11775-11781
    • Asher, S.A.1    Ianoul, A.2    Mix, G.3    Boyden, M.N.4    Karnoup, A.5    Diem, M.6    Schweitzer-Stenner, R.7
  • 25
    • 6344277284 scopus 로고    scopus 로고
    • Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution
    • Ngarize S., Herman H., Adams A., and Howell N. Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution. J. Agric. Food Chem. 52 (2004) 6470-6477
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 6470-6477
    • Ngarize, S.1    Herman, H.2    Adams, A.3    Howell, N.4
  • 26
    • 33750061923 scopus 로고    scopus 로고
    • Proline zwitterion dynamics in solution, glass, and crystalline state
    • Kapitan J., Baumruk V., Kopecky V., Pohl R., and Bour P. Proline zwitterion dynamics in solution, glass, and crystalline state. J. Am. Chem. Soc. 128 (2006) 13451-13462
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13451-13462
    • Kapitan, J.1    Baumruk, V.2    Kopecky, V.3    Pohl, R.4    Bour, P.5
  • 27
    • 33644531529 scopus 로고    scopus 로고
    • Demonstration of the ring conformation in polyproline by the Raman Optical Activity
    • Kapitan J., Baumruk V., and Bour P. Demonstration of the ring conformation in polyproline by the Raman Optical Activity. J. Am. Chem. Soc. 128 (2006) 2438-2443
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2438-2443
    • Kapitan, J.1    Baumruk, V.2    Bour, P.3
  • 28
    • 0032909732 scopus 로고    scopus 로고
    • Raman spectral analysis in the C-H stretching region of proteins and amino acids for investigation of hydrophobic interactions
    • Howell N.K., Arteaga G., Nakai S., and Li-Chan E.C.Y. Raman spectral analysis in the C-H stretching region of proteins and amino acids for investigation of hydrophobic interactions. J. Agric. Food Chem. 47 (1999) 924-933
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 924-933
    • Howell, N.K.1    Arteaga, G.2    Nakai, S.3    Li-Chan, E.C.Y.4
  • 29
    • 28844441969 scopus 로고    scopus 로고
    • Secondary structure of α-synuclein oligomers: characterization by Raman and Atomic Force Microscopy
    • Apetri M.M., Maiti N.C., Zagorski M.G., Carey P.R., and Anderson V.E. Secondary structure of α-synuclein oligomers: characterization by Raman and Atomic Force Microscopy. J. Mol. Biol. 355 (2006) 63-71
    • (2006) J. Mol. Biol. , vol.355 , pp. 63-71
    • Apetri, M.M.1    Maiti, N.C.2    Zagorski, M.G.3    Carey, P.R.4    Anderson, V.E.5
  • 30
    • 34347251868 scopus 로고    scopus 로고
    • FTIR studies of collagen model peptides: complementary experimental and simulation approaches to conformation and unfolding
    • Bryan M., Brauner J., Anderle G., Flach C., Brodsky B., and Mendelsohn R. FTIR studies of collagen model peptides: complementary experimental and simulation approaches to conformation and unfolding. J. Am. Chem. Soc. 129 (2007) 7877-7884
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 7877-7884
    • Bryan, M.1    Brauner, J.2    Anderle, G.3    Flach, C.4    Brodsky, B.5    Mendelsohn, R.6
  • 31
    • 0029860854 scopus 로고    scopus 로고
    • Glycylglycine π-π* and charge transfer transition moment orientations: near-resonance Raman single-crystal measurements
    • Pajcini V., Chen G., Bormett R., Geib S., Li P., Asher S., and Lidiak E. Glycylglycine π-π* and charge transfer transition moment orientations: near-resonance Raman single-crystal measurements. J. Am. Chem. Soc. 118 (1996) 9716-9726
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9716-9726
    • Pajcini, V.1    Chen, G.2    Bormett, R.3    Geib, S.4    Li, P.5    Asher, S.6    Lidiak, E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.