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Volumn 117, Issue 47, 2013, Pages 14625-14634

Site-specific orientation of an a-Helical Peptide Ovispirin-1 from Isotope-Labeled SFG spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ENHANCED SENSITIVITY; HAMILTONIAN APPROACH; POLARIZATION DEPENDENCE; POLARIZATION RESPONSE; SOLID/LIQUID INTERFACES; STRUCTURAL CONSTRAINTS; STRUCTURAL DISORDERS; SUM-FREQUENCY GENERATION;

EID: 84891360718     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp408064b     Document Type: Article
Times cited : (31)

References (67)
  • 1
    • 33645517136 scopus 로고    scopus 로고
    • Elucidation of residue-level structure and dynamics of polypeptides via isotope-edited infrared spectroscopy
    • Decatur, S. M. Elucidation of Residue-Level Structure and Dynamics of Polypeptides via Isotope-Edited Infrared Spectroscopy. Acc. Chem. Res. 2006, 39, 169-175.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 169-175
    • Decatur, S.M.1
  • 4
    • 59649114004 scopus 로고    scopus 로고
    • Gating mechanism of the influenza a m2 channel revealed by 1d and 2d ir spectroscopies
    • Manor, J.; Mukherjee, P.; Lin, Y.-S.; Leonov, H.; Skinner, J. L.; Zanni, M. T.; Arkin, I. T. Gating Mechanism of the Influenza A M2 Channel Revealed by 1D and 2D IR Spectroscopies. Structure 2009, 17, 247-254.
    • (2009) Structure , vol.17 , pp. 247-254
    • Manor, J.1    Mukherjee, P.2    Lin, Y.-S.3    Leonov, H.4    Skinner, J.L.5    Zanni, M.T.6    Arkin, I.T.7
  • 5
    • 79957962090 scopus 로고    scopus 로고
    • Three-dimensional structures by two-dimensional vibrational spectroscopy
    • Remorino, A.; Korendovych, I. V.; Wu, Y.; DeGrado, W. F.; Hochstrasser, R. M. Three-Dimensional Structures by Two-Dimensional Vibrational Spectroscopy. Science 2011, 332, 1206-1209.
    • (2011) Science , vol.332 , pp. 1206-1209
    • Remorino, A.1    Korendovych, I.V.2    Wu, Y.3    DeGrado, W.F.4    Hochstrasser, R.M.5
  • 6
    • 79958861452 scopus 로고    scopus 로고
    • Conformational heterogeneity within the michaelis complex of lactate dehydrogenase
    • Deng, H.; Vu, D. V.; Clinch, K.; Desamero, R.; Dyer, R. B.; Callender, R. Conformational Heterogeneity within the Michaelis Complex of Lactate Dehydrogenase. J. Phys. Chem. B 2011, 115, 7670-7678.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7670-7678
    • Deng, H.1    Vu, D.V.2    Clinch, K.3    Desamero, R.4    Dyer, R.B.5    Callender, R.6
  • 7
    • 26444460186 scopus 로고    scopus 로고
    • The α-helix folds more rapidly at the c-terminus than at the nterminus
    • Pozo Ramajo, A.; Petty, S. A.; Starzyk, A.; Decatur, S. M.; Volk, M. The α-Helix Folds More Rapidly at the C-Terminus than at the NTerminus. J. Am. Chem. Soc. 2005, 127, 13784-13785.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13784-13785
    • Pozo Ramajo, A.1    Petty, S.A.2    Starzyk, A.3    Decatur, S.M.4    Volk, M.5
  • 10
    • 26444514550 scopus 로고    scopus 로고
    • Intersheet rearrangement of polypeptides during nucleation of β-sheet aggregates
    • Petty, S. A.; Decatur, S. M. Intersheet Rearrangement of Polypeptides During Nucleation of β-Sheet Aggregates. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 14272-14277.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14272-14277
    • Petty, S.A.1    Decatur, S.M.2
  • 11
    • 45549085028 scopus 로고    scopus 로고
    • Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from abeta40
    • Kim, Y. S.; Liu, L.; Axelsen, P. H.; Hochstrasser, R. M. Two-Dimensional Infrared Spectra of Isotopically Diluted Amyloid Fibrils from Abeta40. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 7720-7725.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7720-7725
    • Kim, Y.S.1    Liu, L.2    Axelsen, P.H.3    Hochstrasser, R.M.4
  • 12
    • 59849124192 scopus 로고    scopus 로고
    • Empirical amide i vibrational frequency map: Application to 2dir line shapes for isotope-edited membrane peptide bundles
    • Lin, Y.-S.; Shorb, J. M.; Mukherjee, P.; Zanni, M. T.; Skinner, J. L. Empirical Amide I Vibrational Frequency Map: Application to 2DIR Line Shapes for Isotope-Edited Membrane Peptide Bundles. J. Phys. Chem. B 2009, 113, 592-602.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 592-602
    • Lin, Y.-S.1    Shorb, J.M.2    Mukherjee, P.3    Zanni, M.T.4    Skinner, J.5
  • 13
    • 84055193135 scopus 로고    scopus 로고
    • Using infrared spectroscopy of cyanylated cysteine to map the membrane binding structure and orientation of the hybrid antimicrobial peptide cm15
    • Alfieri, K. N.; Vienneau, A. R.; Londergan, C. H. Using Infrared Spectroscopy of Cyanylated Cysteine To Map the Membrane Binding Structure and Orientation of the Hybrid Antimicrobial Peptide CM15. Biochemistry 2011, 50, 11097-11108.
    • (2011) Biochemistry , vol.50 , pp. 11097-11108
    • Alfieri, K.N.1    Vienneau, A.R.2    Londergan, C.H.3
  • 14
    • 0025608693 scopus 로고
    • Polarized fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange
    • Earnest, T. N.; Herzfeld, J.; Rothschild, K. J. Polarized Fourier Transform Infrared Spectroscopy of Bacteriorhodopsin. Transmembrane Alpha Helices are Resistant to Hydrogen/deuterium Exchange. Biophys. J. 1990, 58, 1539-1546.
    • (1990) Biophys. J. , vol.58 , pp. 1539-1546
    • Earnest, T.N.1    Herzfeld, J.2    Rothschild, K.J.3
  • 15
    • 33646123776 scopus 로고    scopus 로고
    • Secondary structure orientation, and oligomerization of phospholemman, a cardiac transmembrane protein
    • Beevers, A. J.; Kukol, A. Secondary Structure, Orientation, and Oligomerization of Phospholemman, a Cardiac Transmembrane Protein. Protein Sci. 2006, 15, 1127-1132.
    • (2006) Protein Sci. , vol.15 , pp. 1127-1132
    • Beevers, A.J.1    Kukol, A.2
  • 16
    • 23244466482 scopus 로고    scopus 로고
    • Disorder influence on linear dichroism analyses of smectic phases
    • Manor, J.; Khattari, Z.; Salditt, T.; Arkin, I. T. Disorder Influence on Linear Dichroism Analyses of Smectic Phases. Biophys. J. 2005, 89, 563-571.
    • (2005) Biophys. J. , vol.89 , pp. 563-571
    • Manor, J.1    Khattari, Z.2    Salditt, T.3    Arkin, I.T.4
  • 17
    • 33846818748 scopus 로고    scopus 로고
    • Multiple orientation of melittin inside a single lipid bilayer determined by combined vibrational spectroscopic studies
    • Chen, X.; Wang, J.; Boughton, A. P.; Kristalyn, C. B.; Chen, Z. Multiple Orientation of Melittin Inside a Single Lipid Bilayer Determined by Combined Vibrational Spectroscopic Studies. J. Am. Chem. Soc. 2007, 129, 1420-1427.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1420-1427
    • Chen, X.1    Wang, J.2    Boughton, A.P.3    Kristalyn, C.B.4    Chen, Z.5
  • 18
    • 80053089071 scopus 로고    scopus 로고
    • Heterotrimeric g protein β1γ2 subunits change orientation upon complex formation with g protein-coupled receptor kinase 2 (grk2) on a model membrane
    • Boughton, A. P.; Yang, P.; Tesmer, V. M.; Ding, B.; Tesmer, J. J. G.; Chen, Z. Heterotrimeric G protein β1γ2 Subunits Change Orientation upon Complex Formation with G Protein-Coupled Receptor Kinase 2 (GRK2) on a Model Membrane. Proc. Natl. Acad. Sci. U.S.A. 2011, 108, E667-673.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Boughton, A.P.1    Yang, P.2    Tesmer, V.3    Ding, B.4    Tesmer, G.J.J.5    Chen, Z.6
  • 19
    • 69949168824 scopus 로고    scopus 로고
    • Orientation determination of protein helical secondary structures using linear and nonlinear vibrational spectroscopy
    • Nguyen, K. T.; Le Clair, S. V.; Ye, S.; Chen, Z. Orientation Determination of Protein Helical Secondary Structures Using Linear and Nonlinear Vibrational Spectroscopy. J. Phys. Chem. B 2009, 113, 12169-12180.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12169-12180
    • Nguyen, K.T.1    Le Clair, S.V.2    Ye, S.3    Chen, Z.4
  • 20
    • 84863232604 scopus 로고    scopus 로고
    • Molecular interactions between cell penetrating peptide pep-1 and model cell membranes
    • Ding, B.; Chen, Z. Molecular Interactions between Cell Penetrating Peptide Pep-1 and Model Cell Membranes. J. Phys. Chem. B 2012, 116, 2545-2552.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 2545-2552
    • Ding, B.1    Chen, Z.2
  • 21
    • 77951697268 scopus 로고    scopus 로고
    • Orientation difference of chemically immobilized and physically adsorbed biological molecules on polymers detected at the solid/liquid interfaces in situ
    • Ye, S.; Nguyen, K. T.; Boughton, A. P.; Mello, C. M.; Chen, Z. Orientation Difference of Chemically Immobilized and Physically Adsorbed Biological Molecules on Polymers Detected at the Solid/Liquid Interfaces in Situ. Langmuir 2010, 26, 6471-6477.
    • (2010) Langmuir , vol.26 , pp. 6471-6477
    • Ye, S.1    Nguyen, K.T.2    Boughton, A.P.3    Mello, C.M.4    Chen, Z.5
  • 22
    • 84859590055 scopus 로고    scopus 로고
    • Observing a model ion channel gating action in model cell membranes in real time in situ: Membrane potential change induced alamethicin orientation change
    • Ye, S.; Li, H.; Wei, F.; Jasensky, J.; Boughton, A. P.; Yang, P.; Chen, Z. Observing a Model Ion Channel Gating Action in Model Cell Membranes in Real Time in Situ: Membrane Potential Change Induced Alamethicin Orientation Change. J. Am. Chem. Soc. 2012, 134, 6237-6243.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6237-6243
    • Ye, S.1    Li, H.2    Wei, F.3    Jasensky, J.4    Boughton, A.P.5    Yang, P.6    Chen, Z.7
  • 23
    • 77953965202 scopus 로고    scopus 로고
    • Orientation determination of interfacial β-sheet structures in situ
    • Nguyen, K. T.; King, J. T.; Chen, Z. Orientation Determination of Interfacial β-Sheet Structures in Situ. J. Phys. Chem. B 2010, 114, 8291-8300.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8291-8300
    • Nguyen, K.T.1    King, J.T.2    Chen, Z.3
  • 24
    • 17044433851 scopus 로고    scopus 로고
    • Detection of chiral sum frequency generation vibrational spectra of proteins and peptides at interfaces in situ
    • Wang, J.; Chen, X.; Clarke, M. L.; Chen, Z. Detection of Chiral Sum Frequency Generation Vibrational Spectra of Proteins and Peptides at Interfaces in Situ. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 4978-4983.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 4978-4983
    • Wang, J.1    Chen, X.2    Clarke, M.L.3    Chen, Z.4
  • 25
    • 77951026783 scopus 로고    scopus 로고
    • In situ misfolding of human islet amyloid polypeptide at interfaces probed by vibrational sum frequency generation
    • Fu, L.; Ma, G.; Yan, E. C. Y. In Situ Misfolding of Human Islet Amyloid Polypeptide at Interfaces Probed by Vibrational Sum Frequency Generation. J. Am. Chem. Soc. 2010, 132, 5405-5412.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5405-5412
    • Fu, L.1    Ma, G.2    Yan, E.C.Y.3
  • 26
    • 84874884712 scopus 로고    scopus 로고
    • Chiral sum frequency generation for in situ probing proton exchange in antiparallel β-sheets at interfaces
    • Fu, L.; Xiao, D.; Wang, Z.; Batista, V. S.; Yan, E. C. Y. Chiral Sum Frequency Generation for In Situ Probing Proton Exchange in Antiparallel β-Sheets at Interfaces. J. Am. Chem. Soc. 2013, 135, 3592-3598.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 3592-3598
    • Fu, L.1    Xiao, D.2    Wang, Z.3    Batista, V.S.4    Yan, E.C.Y.5
  • 27
    • 77955786270 scopus 로고    scopus 로고
    • Sum frequency generation and solid-state nmr study of the structure, orientation, and dynamics of polystyrene-adsorbed peptides
    • Weidner, T.; Breen, N. F.; Li, K.; Drobny, G. P.; Castner, D. G. Sum Frequency Generation and Solid-state NMR Study of the Structure, Orientation, and Dynamics of Polystyrene-Adsorbed Peptides. Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 13288-13293.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13288-13293
    • Weidner, T.1    Breen, N.F.2    Li, K.3    Drobny, G.P.4    Castner, D.5
  • 28
    • 77749320965 scopus 로고    scopus 로고
    • Probing the orientation and conformation of α-helix and β-strand model peptides on self-assembled monolayers using sum frequency generation and nexafs spectroscopy
    • Weidner, T.; Apte, J. S.; Gamble, L. J.; Castner, D. G. Probing the Orientation and Conformation of α-Helix and β-Strand Model Peptides on Self-Assembled Monolayers Using Sum Frequency Generation and NEXAFS Spectroscopy. Langmuir 2010, 26, 3433-3440.
    • (2010) Langmuir , vol.26 , pp. 3433-3440
    • Weidner, T.1    Apte, J.S.2    Gamble, L.J.3    Castner, D.G.4
  • 29
    • 0036231767 scopus 로고    scopus 로고
    • Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides
    • Sawai, M. V.; Waring, A. J.; Kearney, W. R.; McCray, P. B.; Forsyth, W. R.; Lehrer, R. I.; Tack, B. F. Impact of Single-Residue Mutations on the Structure and Function of Ovispirin/Novispirin Antimicrobial Peptides. Protein Eng. 2002, 15, 225-232.
    • (2002) Protein Eng. , vol.15 , pp. 225-232
    • Sawai, M.V.1    Waring, A.J.2    Kearney, W.R.3    McCray, P.B.4    Forsyth, W.R.5    Lehrer, R.I.6    Tack, B.F.7
  • 30
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state nmr spectroscopy
    • Yamaguchi, S.; Huster, D.; Waring, A.; Lehrer, R. I.; Kearney, W.; Tack, B. F.; Hong, M. Orientation and Dynamics of an Antimicrobial Peptide in the Lipid Bilayer by Solid-State NMR Spectroscopy. Biophys. J. 2001, 81, 2203-2214.
    • (2001) Biophys. J. , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 31
    • 33645420002 scopus 로고    scopus 로고
    • In situ adsorption studies of a 14-amino acid leucine-lysine peptide onto hydrophobic polystyrene and hydrophilic silica surfaces using quartz crystal microbalance, atomic force microscopy, and sum frequency generation vibrational spectroscopy
    • Mermut, O.; Phillips, D. C.; York, R. L.; McCrea, K. R.; Ward, R. S.; Somorjai, G. In Situ Adsorption Studies of a 14-Amino Acid Leucine-Lysine Peptide onto Hydrophobic Polystyrene and Hydrophilic Silica Surfaces Using Quartz Crystal Microbalance, Atomic Force Microscopy, and Sum Frequency Generation Vibrational Spectroscopy. J. Am. Chem. Soc. 2006, 128, 3598-3607.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3598-3607
    • Mermut, O.1    Phillips, D.C.2    York, R.L.3    McCrea, K.R.4    Ward, R.S.5    Somorjai, G.6
  • 32
    • 33646441898 scopus 로고    scopus 로고
    • Theoretical modeling of interface specific vibrational spectroscopy: Methods and applications to aqueous interfaces
    • Perry, A.; Neipert, C. Space, B. Theoretical Modeling of Interface Specific Vibrational Spectroscopy: Methods and Applications to Aqueous Interfaces. Chem. Rev. 2006, 106, 1234-1258.
    • (2006) Chem. Rev. , vol.106 , pp. 1234-1258
    • Perry, A.1    Neipert, C.2    Space, B.3
  • 33
    • 3142763239 scopus 로고    scopus 로고
    • Direct measurement of the transbilayer movement of phospholipids by sum-frequency vibrational spectroscopy
    • Liu, J.; Conboy, J. C. Direct Measurement of the Transbilayer Movement of Phospholipids by Sum-Frequency Vibrational Spectroscopy. J. Am. Chem. Soc. 2004, 126, 8376-8377.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8376-8377
    • Liu, J.1    Conboy, J.C.2
  • 34
    • 36148999406 scopus 로고    scopus 로고
    • Dangling od confined in a langmuir monolayer
    • Ma, G.; Chen, X.; Allen, H. C. Dangling OD Confined in a Langmuir Monolayer. J. Am. Chem. Soc. 2007, 129, 14053-14057.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14053-14057
    • Ma, G.1    Chen, X.2    Allen, H.C.3
  • 35
    • 84880765556 scopus 로고    scopus 로고
    • Determining in situ protein conformation and orientation from the amide-i sum-frequency generation spectrum: Theory and experiment
    • Roeters, S. J.; van Dijk, C. N.; Torres-Knoop, A.; Backus, E. H. G.; Campen, R. k.; Bonn, M.; Woutersen, S. Determining in Situ Protein Conformation and Orientation from the Amide-I Sum-Frequency Generation Spectrum: Theory and Experiment. J. Phys. Chem. A 2013, 117, 6311-6322.
    • (2013) J. Phys. Chem. A , vol.117 , pp. 6311-6322
    • Roeters, S.J.1    Van Dijk, C.N.2    Torres-Knoop, A.3    Backus, E.H.G.4    Campen, R.5    Bonn, M.6    Woutersen, S.7
  • 37
    • 78049283410 scopus 로고    scopus 로고
    • Specific anion effects on water structure adjacent to protein monolayers
    • Chen, X.; Flores, S. C.; Lim, S.-M.; Zhang, Y.; Yang, T.; Kherb, J.; Cremer, P. S. Specific Anion Effects on Water Structure Adjacent to Protein Monolayers. Langmuir 2010, 26, 16447-16454.
    • (2010) Langmuir , vol.26 , pp. 16447-16454
    • Chen, X.1    Flores, S.C.2    Lim, S.-M.3    Zhang, Y.4    Yang, T.5    Kherb, J.6    Cremer, P.S.7
  • 38
    • 84866425464 scopus 로고    scopus 로고
    • The polyphenol egcg inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution
    • Engel, M. F. M.; vanden Akker, C. C.; Schleeger, M.; Velikov, K. P.; Koenderink, G. H.; Bonn, M. The Polyphenol EGCG Inhibits Amyloid Formation Less Efficiently at Phospholipid Interfaces than in Bulk Solution. J. Am. Chem. Soc. 2012, 134, 14781-14788.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 14781-14788
    • Engel, M.F.M.1    Vanden Akker, C.2    Schleeger, M.3    Velikov, K.4    Koenderink, G.5    Bonn, M.6
  • 39
    • 84870858388 scopus 로고    scopus 로고
    • In situ molecular-level insights into the interfacial structure changes of membrane-associated prion protein fragment [118-135] investigated by sum frequency generation vibrational spectroscopy
    • Li, H.; Ye, S.; Wei, F.; Ma, S.; Luo, Y. In Situ Molecular-Level Insights into the Interfacial Structure Changes of Membrane-Associated Prion Protein Fragment [118-135] Investigated by Sum Frequency Generation Vibrational Spectroscopy. Langmuir 2012, 28, 16979-16988.
    • (2012) Langmuir , vol.28 , pp. 16979-16988
    • Li, H.1    Ye, S.2    Wei, F.3    Ma, S.4    Luo, Y.5
  • 40
    • 0041520556 scopus 로고    scopus 로고
    • Detection of amide i signals of interfacial proteins in situ using sfg
    • Wang, J.; Even, M. A.; Chen, X.; Schmaier, A. H.; Waite, J. H.; Chen, Z. Detection of Amide I Signals of Interfacial Proteins in Situ Using SFG. J. Am. Chem. Soc. 2003, 125, 9914-9915.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9914-9915
    • Wang, J.1    Even, M.A.2    Chen, X.3    Schmaier, A.H.4    Waite, J.H.5    Chen, Z.6
  • 42
    • 84879050067 scopus 로고    scopus 로고
    • Extracting structural information from the polarization dependence of one-and two-dimensional sum frequency generation spectra
    • Laaser, J. E.; Zanni, M. T. Extracting Structural Information from the Polarization Dependence of One-and Two-Dimensional Sum Frequency Generation Spectra. J. Phys. Chem. A 2013, 117, 5875-5890.
    • (2013) J. Phys. Chem. A , vol.117 , pp. 5875-5890
    • Laaser, J.E.1    Zanni, M.T.2
  • 43
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm, L. K.; Tatulian, S. A. Infrared Spectroscopy of Proteins and Peptides in Lipid Bilayers. Q. Rev. Biophys. 1997, 30, 365-429.
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 44
    • 11844262057 scopus 로고    scopus 로고
    • Spectroscopic evidence for backbone desolvation of helical peptides by 2 ,2,2-trifluoroethanol: An isotope-edited ftir study
    • Starzyk, A.; Barber-Armstrong, W.; Sridharan, M.; Decatur, S. M. Spectroscopic Evidence for Backbone Desolvation of Helical Peptides by 2,2,2-Trifluoroethanol: an Isotope-Edited FTIR Study. Biochemistry 2005, 44, 369-376.
    • (2005) Biochemistry , vol.44 , pp. 369-376
    • Starzyk, A.1    Barber-Armstrong, W.2    Sridharan, M.3    Decatur, S.M.4
  • 45
    • 78049402251 scopus 로고    scopus 로고
    • Probing the spontaneous membrane insertion of a tail-anchored membrane protein by sum frequency generation spectroscopy
    • Nguyen, K. T.; Soong, R.; Lm, S.-C.; Waskell, L.; Ramamoorthy, A.; Chen, Z. Probing the Spontaneous Membrane Insertion of a Tail-Anchored Membrane Protein by Sum Frequency Generation Spectroscopy. J. Am. Chem. Soc. 2010, 132, 15112-15115.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15112-15115
    • Nguyen, K.T.1    Soong, R.2    Lm, S.-C.3    Waskell, L.4    Ramamoorthy, A.5    Chen, Z.6
  • 47
    • 0041638532 scopus 로고    scopus 로고
    • Infrared spectra of amide groups in α-helical proteins: Evidence for hydrogen bonding between helices and water
    • Manas, E. S.; Getahun, Z.; Wright, W. W.; DeGrado, W. F.; Vanderkooi, J. M. Infrared Spectra of Amide Groups in α-Helical Proteins: Evidence for Hydrogen Bonding between Helices and Water. J. Am. Chem. Soc. 2000, 122, 9883-9890.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9883-9890
    • Manas, E.S.1    Getahun, Z.2    Wright, W.W.3    DeGrado, W.F.4    Vanderkooi, J.M.5
  • 48
    • 34548173919 scopus 로고    scopus 로고
    • Phase-sensitive sum-frequency vibrational spectroscopy and its application to studies of interfacial alkyl chains
    • Ji, N.; Ostroverkhov, V.; Chen, C.-Y.; Shen, R.-Y. Phase-Sensitive Sum-frequency Vibrational Spectroscopy and Its Application to Studies of Interfacial Alkyl Chains. J. Am. Chem. Soc. 2007, 129, 10056-10057.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10056-10057
    • Ji, N.1    Ostroverkhov, V.2    Chen, C.-Y.3    Shen, R.-Y.4
  • 50
    • 66749113458 scopus 로고    scopus 로고
    • Direct evidence for orientational flip-flop of water molecules at charged interfaces: A heterodyne-detected vibrational sum frequency generation study
    • Nihonyanagi, S.; Yamaguchi, S.; Tahara, T. Direct Evidence for Orientational Flip-Flop of Water Molecules at Charged Interfaces: A Heterodyne-Detected Vibrational Sum Frequency Generation Study. J. Chem. Phys. 2009, 130, 204704.
    • (2009) J Chem. Phys. , vol.130 , pp. 204704
    • Nihonyanagi, S.1    Yamaguchi, S.2    Tahara, T.3
  • 51
    • 79952747921 scopus 로고    scopus 로고
    • Time-domain sfg spectroscopy using mid-ir pulse shaping: Practical and intrinsic advantages
    • Laaser, J. E.; Xiong, W.; Zanni, M. T. Time-Domain SFG Spectroscopy Using Mid-IR Pulse Shaping: Practical and Intrinsic Advantages. J. Phys. Chem. B 2011, 115, 2536-2546.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 2536-2546
    • Laaser, J.E.1    Xiong, W.2    Zanni, M.3
  • 52
    • 0000835650 scopus 로고
    • The vibration spectra of helical molecules: Infra-red and raman selection rules, intensities and approximate frequencies
    • Higgs, P. W. The Vibration Spectra of Helical Molecules: Infra-Red and Raman Selection Rules, Intensities and Approximate Frequencies. Proc. R. Soc. London 1953, 220, 472-485.
    • (1953) Proc. R. Soc. London , vol.220 , pp. 472-485
    • Higgs, P.W.1
  • 53
    • 36849130297 scopus 로고
    • Optical rotatory dispersion of helical polymers
    • Moffitt, W. Optical Rotatory Dispersion of Helical Polymers. J. Chem. Phys. 1956, 25, 467.
    • (1956) J Chem. Phys. , vol.25 , pp. 467
    • Moffitt, W.1
  • 54
    • 24644433652 scopus 로고    scopus 로고
    • Vibrational spectroscopic characteristics of secondary structure polypeptides in liquid water: Constrained md simulation studies
    • Choi, J.-H.; Hahn, S.; Cho, M. Vibrational Spectroscopic Characteristics of Secondary Structure Polypeptides in Liquid Water: Constrained MD Simulation Studies. Int. J. Quantum Chem. 2005, 104, 616-634.
    • (2005) Int. J. Quantum Chem. , vol.104 , pp. 616-634
    • Choi, J.-H.1    Hahn, S.2    Cho, M.3
  • 55
    • 33846090722 scopus 로고    scopus 로고
    • Structural disorder of the cd3 transmembrane domain studied with 2d ir spectroscopy and molecular dynamics simulations
    • Mukherjee, P.; Kass, I.; Arkin, I. T.; Zanni, M. T. Structural Disorder of the CD3ζ Transmembrane Domain Studied with 2D IR Spectroscopy and Molecular Dynamics Simulations. J. Phys. Chem. B 2006, 110, 24740-24749.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 24740-24749
    • Mukherjee, P.1    Kass, I.2    Arkin, I.T.3    Zanni, M.T.4
  • 56
    • 0036071621 scopus 로고    scopus 로고
    • A structure for the trimeric mhc class ii-associated invariant chain transmembrane domain
    • Kuko1, A.; Torres, J.; Arkin, I. T. A Structure for the Trimeric MHC Class II-Associated Invariant Chain Transmembrane Domain. J. Mol. Biol. 2002, 320, 1109-1117.
    • (2002) J. Mol. Biol. , vol.320 , pp. 1109-1117
    • Kuko, A.1    Torres, J.2    Arkin, I.T.3
  • 58
    • 79961051077 scopus 로고    scopus 로고
    • Interpretation of the water surface vibrational sum-frequency spectrum
    • Pieniazek, P. A.; Tainter, C. J.; Skinner, J. L. Interpretation of the Water Surface Vibrational Sum-Frequency Spectrum. J. Chem. Phys. 2011, 135, 044701.
    • (2011) J Chem. Phys. , vol.135 , pp. 044701
    • Pieniazek, P.A.1    Tainter, C.J.2    Skinner, J.L.3
  • 60
    • 34250588360 scopus 로고
    • Infrared spectra of high polymers
    • Krimm, S. Infrared Spectra of High Polymers. Fortschr. Hochpolym.-Forsh., Bd. 1960, 2, 241-254.
    • (1960) Fortschr. Hochpolym.-Forsh., Bd. , Issue.2 , pp. 241-254
    • Krimm, S.1
  • 61
    • 0025922973 scopus 로고
    • Orientation of specifically 13co labeled phosphatidylcholine multilayers from polarized attenuated total reflection ft-ir spectroscopy
    • Hubner, W.; Mantsch, H. H. Orientation of Specifically 13CO Labeled Phosphatidylcholine Multilayers from Polarized Attenuated Total Reflection FT-IR Spectroscopy. Biophys. J. 1991, 59, 1261-1272.
    • (1991) Biophys. J , vol.59 , pp. 1261-1272
    • Hubner, W.1    Mantsch, H.H.2
  • 63
    • 61849177109 scopus 로고    scopus 로고
    • Expressed protein ligation (epl) in the study of signal transduction, ion conduction, and chromatin biology
    • Flavell, R. R.; Muir, T. W. Expressed Protein Ligation (EPL) in the Study of Signal Transduction, Ion Conduction, and Chromatin Biology. Acc. Chem. Res. 2009, 42, 107-116.
    • (2009) Acc. Chem. Res. , vol.42 , pp. 107-116
    • Flavell, R.R.1    Muir, T.2
  • 64
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P. E.; Muir, T. W.; Clark-Lewis, I.; Kent, S. B. Synthesis of Proteins by Native Chemical Ligation. Science 1994, 266, 776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 65
    • 84868549643 scopus 로고    scopus 로고
    • Structural and sequence analysis of the human γd-crystallin amyloid fibril core using 2d ir spectroscopy, segmental 13c labeling, and mass spectrometry
    • Moran, S. D.; Decatur, S. M.; Zanni, M. T. Structural and Sequence Analysis of the Human γD-Crystallin Amyloid Fibril Core Using 2D IR Spectroscopy, Segmental 13C Labeling, and Mass Spectrometry. J. Am. Chem. Soc. 2012, 134, 18410-18416.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 18410-18416
    • Moran, S.D.1    Decatur, S.M.2    Zanni, M.3
  • 67
    • 70349781906 scopus 로고    scopus 로고
    • Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: A combined fluorescence, ir and molecular dynamics study
    • Taskent-Sezgin, H.; Chung, J.; Patsalo, V.; Miyake-Stoner, S. J.; Miller, A. M.; Brewer, S. H.; Mehl, R. A.; Greene, D. F.; Raleigh, D. P.; Carrico, I. Interpretation of p-Cyanophenylalanine Fluorescence in Proteins in Terms of Solvent Exposure and Contribution of Side-Chain Quenchers: a Combined Fluorescence, IR and Molecular Dynamics Study. Biochemistry 2009, 48, 9040-9046.
    • (2009) Biochemistry , vol.48 , pp. 9040-9046
    • Taskent-Sezgin, H.1    Chung, J.2    Patsalo, V.3    Miyake-Stoner, S.J.4    Miller, A.M.5    Brewer, S.H.6    Mehl, R.A.7    Greene, D.F.8    Raleigh, D.P.9    Carrico, I.10


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