메뉴 건너뛰기




Volumn 109, Issue 38, 2012, Pages 15301-15306

Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography

Author keywords

Crystal; Hydrogen deuterium exchange; Neutron structure; PDB 4FC1; Solvent

Indexed keywords

CRAMBIN; DEUTERIUM; PROTEIN; UNCLASSIFIED DRUG;

EID: 84866545609     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1208341109     Document Type: Article
Times cited : (50)

References (43)
  • 2
    • 70449585313 scopus 로고    scopus 로고
    • Neutron macromolecular crystallography
    • Blakeley MP (2009) Neutron macromolecular crystallography. Crystallogr Rev 15:157-218.
    • (2009) Crystallogr Rev , vol.15 , pp. 157-218
    • Blakeley, M.P.1
  • 3
    • 0019889789 scopus 로고
    • Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin
    • Kossiakoff AA, Spencer SA (1981) Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin. Biochemistry 20:6462-6474.
    • (1981) Biochemistry , vol.20 , pp. 6462-6474
    • Kossiakoff, A.A.1    Spencer, S.A.2
  • 7
    • 58849161928 scopus 로고    scopus 로고
    • Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement
    • Blum M-M, et al. (2009) Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement. Proc Natl Acad Sci USA 106:713-718.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 713-718
    • Blum, M.-M.1
  • 8
    • 74949121428 scopus 로고    scopus 로고
    • Neutron structure of human carbonic anhydrase II: Implications for proton transfer
    • Fisher Z, et al. (2010) Neutron structure of human carbonic anhydrase II: Implications for proton transfer. Biochemistry 49:415-421.
    • (2010) Biochemistry , vol.49 , pp. 415-421
    • Fisher, Z.1
  • 9
    • 77953546976 scopus 로고    scopus 로고
    • Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: A joint X-ray and neutron diffraction study
    • Kovalevsky AY, et al. (2010) Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: A joint X-ray and neutron diffraction study. Structure 18:688-699.
    • (2010) Structure , vol.18 , pp. 688-699
    • Kovalevsky, A.Y.1
  • 10
    • 80155203797 scopus 로고    scopus 로고
    • Neutron structure of human carbonic anhydrase II: A hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0
    • Fisher Z, et al. (2011) Neutron structure of human carbonic anhydrase II: A hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0. Biochemistry 50:9421-9423.
    • (2011) Biochemistry , vol.50 , pp. 9421-9423
    • Fisher, Z.1
  • 11
    • 79953791129 scopus 로고    scopus 로고
    • Neutron structure of type-III antifreeze protein allows the reconstruction of AFP-ice interface
    • Howard EI, et al. (2011) Neutron structure of type-III antifreeze protein allows the reconstruction of AFP-ice interface. J Mol Recognit 24:724-732.
    • (2011) J Mol Recognit , vol.24 , pp. 724-732
    • Howard, E.I.1
  • 12
    • 79952175807 scopus 로고    scopus 로고
    • X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex
    • Kawamura K, et al. (2011) X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex. Acta Crystallogr D 67:140-148.
    • (2011) Acta Crystallogr D , vol.67 , pp. 140-148
    • Kawamura, K.1
  • 13
    • 79961217081 scopus 로고    scopus 로고
    • Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values
    • Kovalevsky AY, et al. (2011) Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values. Angew Chem Int Ed 50:7520-7523.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 7520-7523
    • Kovalevsky, A.Y.1
  • 14
    • 78651374505 scopus 로고    scopus 로고
    • The active site protonation states of perdeuterated Toho-1 b-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation
    • Tomanicek S, et al. (2011) The active site protonation states of perdeuterated Toho-1 b-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation. FEBS Lett 585:364-368.
    • (2011) FEBS Lett , vol.585 , pp. 364-368
    • Tomanicek, S.1
  • 15
    • 84857031868 scopus 로고    scopus 로고
    • Hydrogen-bond network and pH sensitivity in transthyretin: Neutron crystal structure of human transthyretin
    • Yokoyama T, et al. (2012) Hydrogen-bond network and pH sensitivity in transthyretin: Neutron crystal structure of human transthyretin. J Struct Biol 177:283-290.
    • (2012) J Struct Biol , vol.177 , pp. 283-290
    • Yokoyama, T.1
  • 16
    • 0021760668 scopus 로고
    • Effect of protein packing structure on side-chain methyl rotor conformations
    • Kossiakoff AA, Shteyn S (1984) Effect of protein packing structure on side-chain methyl rotor conformations. Nature 311:582-583.
    • (1984) Nature , vol.311 , pp. 582-583
    • Kossiakoff, A.A.1    Shteyn, S.2
  • 17
    • 0031566067 scopus 로고    scopus 로고
    • Zero point motion of the librating methyl group in p-hydroxyacetanilide
    • Wilson CC (1997) Zero point motion of the librating methyl group in p-hydroxyacetanilide. Chem Phys Lett 280:531-534.
    • (1997) Chem Phys Lett , vol.280 , pp. 531-534
    • Wilson, C.C.1
  • 18
    • 0020488766 scopus 로고
    • Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique
    • Kossiakoff AA (1982) Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique. Nature 296:713-721.
    • (1982) Nature , vol.296 , pp. 713-721
    • Kossiakoff, A.A.1
  • 19
    • 0027459475 scopus 로고
    • Atomic resolution (0.83 Å) crystal structure of the hydrophobic protein crambin at 130 K
    • DOI 10.1006/jmbi.1993.1143
    • Teeter MM, Roe SM, Heo NH (1993) Atomic resolution (0.83 Å) crystal structure of the hydrophobic protein crambin at 130 K. J Mol Biol 230:292-311. (Pubitemid 23093564)
    • (1993) Journal of Molecular Biology , vol.230 , Issue.1 , pp. 292-311
    • Teeter, M.M.1    Roe, S.M.2    Heo, N.H.3
  • 20
    • 79955112216 scopus 로고    scopus 로고
    • Crystal structure of the small protein crambin at 0.48 Å resolution
    • Schmidt A, Teeter M, Weckert E, Lamzin VS (2011) Crystal structure of the small protein crambin at 0.48 Å resolution. Acta Crystallogr F 67:424-428.
    • (2011) Acta Crystallogr F , vol.67 , pp. 424-428
    • Schmidt, A.1    Teeter, M.2    Weckert, E.3    Lamzin, V.S.4
  • 23
    • 66249139220 scopus 로고    scopus 로고
    • Generalized X-ray and neutron crystallographic analysis: More accurate and complete structures for biological macromolecules
    • Adams PD, Mustyakimov M, Afonine PV, Langan P (2009) Generalized X-ray and neutron crystallographic analysis: More accurate and complete structures for biological macromolecules. Acta Crystallogr D 65:567-573.
    • (2009) Acta Crystallogr D , vol.65 , pp. 567-573
    • Adams, P.D.1    Mustyakimov, M.2    Afonine, P.V.3    Langan, P.4
  • 24
    • 84863126254 scopus 로고    scopus 로고
    • Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin
    • Chen JC-H, et al. (2012) Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin. Acta Crystallogr F 68:119-123.
    • (2012) Acta Crystallogr F , vol.68 , pp. 119-123
    • Chen, J.C.-H.1
  • 25
    • 0022349985 scopus 로고
    • Study of ethanol-lysozyme interactions using neutron diffraction
    • DOI 10.1021/bi00342a026
    • Lehmann MS, Mason SA, McIntyre GJ (1985) Study of ethanol-lysozyme interactions using neutron diffraction. Biochemistry 24:5862-5869. (Pubitemid 16203026)
    • (1985) Biochemistry , vol.24 , Issue.21 , pp. 5862-5869
    • Lehmann, M.S.1    Mason, S.A.2    McIntyre, G.J.3
  • 27
    • 79958022738 scopus 로고    scopus 로고
    • High-resolution neutron crystallographic studies of the hydration of the coenzyme cob(II)almin
    • Jogl G, et al. (2011) High-resolution neutron crystallographic studies of the hydration of the coenzyme cob(II)almin. Acta Crystallogr D 67:584-591.
    • (2011) Acta Crystallogr D , vol.67 , pp. 584-591
    • Jogl, G.1
  • 28
    • 78049479623 scopus 로고    scopus 로고
    • Joint X-ray and neutron refinement with phenix.refine
    • Afonine P, et al. (2010) Joint X-ray and neutron refinement with phenix.refine. Acta Crystallogr D 66:1153-1163.
    • (2010) Acta Crystallogr D , vol.66 , pp. 1153-1163
    • Afonine, P.1
  • 30
    • 0035971221 scopus 로고    scopus 로고
    • Strength of the CαH-O hydrogen bond of amino acids
    • Scheiner S, Kar T, Gu Y (2001) Strength of the CαH-O hydrogen bond of amino acids. J Biol Chem 278:9832- 9837.
    • (2001) J Biol Chem , vol.278 , pp. 9832-9837
    • Scheiner, S.1    Kar, T.2    Gu, Y.3
  • 32
    • 0042305020 scopus 로고    scopus 로고
    • High resolution neutron protein crystallography. Hydrogen and hydration in proteins
    • Niimura N, Chatake T, Ostermann A, Kurihara K, Tanaka I (2003) High resolution neutron protein crystallography. Hydrogen and hydration in proteins. Z Krist 218:96-107.
    • (2003) Z Krist , vol.218 , pp. 96-107
    • Niimura, N.1    Chatake, T.2    Ostermann, A.3    Kurihara, K.4    Tanaka, I.5
  • 33
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D, Tsai C-J, Nussinov R (1997) Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 10:999-1012. (Pubitemid 28004646)
    • (1997) Protein Engineering , vol.10 , Issue.9 , pp. 999-1012
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 34
    • 61449124041 scopus 로고    scopus 로고
    • Lone pair...pi interactions between water oxygens and aromatic residues: Quantum chemical studies based on high-resolution protein structures and model compounds
    • Jain A, Ramanathan V, Sankararamakrishnan R (2009) Lone pair...pi interactions between water oxygens and aromatic residues: Quantum chemical studies based on high-resolution protein structures and model compounds. Protein Sci 18:595-605.
    • (2009) Protein Sci , vol.18 , pp. 595-605
    • Jain, A.1    Ramanathan, V.2    Sankararamakrishnan, R.3
  • 35
    • 77952040164 scopus 로고    scopus 로고
    • Unambiguous determination of H-atom positions: Comparing results from neutron and high-resolution X-ray crystallography
    • Gardberg AS, et al. (2010) Unambiguous determination of H-atom positions: Comparing results from neutron and high-resolution X-ray crystallography. Acta Crystallogr D 66:558-567.
    • (2010) Acta Crystallogr D , vol.66 , pp. 558-567
    • Gardberg, A.S.1
  • 37
    • 84857827085 scopus 로고    scopus 로고
    • Rapid visualization of hydrogen positions in protein neutron crystallographic structures
    • Munshi P, et al. (2012) Rapid visualization of hydrogen positions in protein neutron crystallographic structures. Acta Crystallogr D 68:35-41.
    • (2012) Acta Crystallogr D , vol.68 , pp. 35-41
    • Munshi, P.1
  • 38
    • 79953902483 scopus 로고    scopus 로고
    • Reintroducing electrostatics into macromolecular crystallographic refinement: Application to neutron crystallography and DNA hydration
    • Fenn T, et al. (2011) Reintroducing electrostatics into macromolecular crystallographic refinement: Application to neutron crystallography and DNA hydration. Structure 19:523-533.
    • (2011) Structure , vol.19 , pp. 523-533
    • Fenn, T.1
  • 40
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath JW (1999) The finer things in X-ray diffraction data collection. Acta Crystallogr D 55:1718-1725.
    • (1999) Acta Crystallogr D , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 41
    • 3543087500 scopus 로고    scopus 로고
    • Protein crystallography with spallation neutrons: Collecting and processing wavelength-resolved Laue protein data
    • Langan P, Greene G (2004) Protein crystallography with spallation neutrons: Collecting and processing wavelength-resolved Laue protein data. J Appl Crystallogr 37:253-257.
    • (2004) J Appl Crystallogr , vol.37 , pp. 253-257
    • Langan, P.1    Greene, G.2
  • 42
    • 0001475908 scopus 로고
    • The recording and analysis of synchrotron X-radiation Laue diffraction photographs
    • Helliwell JR, et al. (1989) The recording and analysis of synchrotron X-radiation Laue diffraction photographs. J Appl Crystallogr 22:483-497.
    • (1989) J Appl Crystallogr , vol.22 , pp. 483-497
    • Helliwell, J.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.