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Volumn 376, Issue 1, 2008, Pages 32-35

An abnormal pKa value of internal histidine of the insulin molecule revealed by neutron crystallographic analysis

Author keywords

Histidine; Insulin; Neutron crystallography; Polymerization; Protonation

Indexed keywords

HISTIDINE; PIG INSULIN; ZINC ION;

EID: 52049087315     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.08.071     Document Type: Article
Times cited : (16)

References (20)
  • 1
    • 77956751025 scopus 로고
    • Insulin: the structure in the crystal and its reflection in chemistry and biology
    • Blundell T., Dodson G., Hodgkin D., and Mercola D. Insulin: the structure in the crystal and its reflection in chemistry and biology. Adv. Protein Chem. 26 (1972) 279-402
    • (1972) Adv. Protein Chem. , vol.26 , pp. 279-402
    • Blundell, T.1    Dodson, G.2    Hodgkin, D.3    Mercola, D.4
  • 4
    • 0018176030 scopus 로고
    • Zinc-free cubic pig insulin: crystallization and structure determination
    • Dodson E.J., Dodson G.G., Lewitova A., and Sabesan M. Zinc-free cubic pig insulin: crystallization and structure determination. J. Mol. Biol. 125 (1978) 387-396
    • (1978) J. Mol. Biol. , vol.125 , pp. 387-396
    • Dodson, E.J.1    Dodson, G.G.2    Lewitova, A.3    Sabesan, M.4
  • 8
    • 0030715546 scopus 로고    scopus 로고
    • Neutron laue diffraction does it faster
    • Helliwell J.R. Neutron laue diffraction does it faster. Nat. Struct. Biol. 4 (1997) 874-876
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 874-876
    • Helliwell, J.R.1
  • 9
    • 0032823529 scopus 로고    scopus 로고
    • Neutrons expand the field of structural biology
    • Niimura N. Neutrons expand the field of structural biology. Curr. Opin. Struct. Biol. 9 (2003) 602-608
    • (2003) Curr. Opin. Struct. Biol. , vol.9 , pp. 602-608
    • Niimura, N.1
  • 10
    • 0036293241 scopus 로고    scopus 로고
    • Neutron diffraction studies on proteins
    • Tsyba I., and Bau R. Neutron diffraction studies on proteins. Chemtracts 15 (2002) 233-257
    • (2002) Chemtracts , vol.15 , pp. 233-257
    • Tsyba, I.1    Bau, R.2
  • 11
    • 2142854125 scopus 로고    scopus 로고
    • Protein crystallography with spallation neutrons
    • Schoenborn B.P., and Langan P. Protein crystallography with spallation neutrons. J. Synchrotron Radiat. 11 (2004) 80-82
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 80-82
    • Schoenborn, B.P.1    Langan, P.2
  • 12
    • 32044434962 scopus 로고    scopus 로고
    • Recent results on hydrogen and hydration in biology studied by neutron macromolecular crystallography
    • Niimura N., Arai S., Kurihara K., Chatake T., Tanaka I., and Bau R. Recent results on hydrogen and hydration in biology studied by neutron macromolecular crystallography. Cell. Mol. Life Sci. 63 (2006) 285-300
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 285-300
    • Niimura, N.1    Arai, S.2    Kurihara, K.3    Chatake, T.4    Tanaka, I.5    Bau, R.6
  • 14
    • 2142692238 scopus 로고    scopus 로고
    • Crystallization of a large single crystal of cubic insulin for neutron protein crystallography
    • Maeda M., Chatake T., Tanaka I., Ostermann A., and Niimura N. Crystallization of a large single crystal of cubic insulin for neutron protein crystallography. J. Synchrotron Radiat. 11 (2004) 41-44
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 41-44
    • Maeda, M.1    Chatake, T.2    Tanaka, I.3    Ostermann, A.4    Niimura, N.5
  • 15
    • 0036098934 scopus 로고    scopus 로고
    • A high-performance neutron diffractometer for biological crystallography (BIX-3)
    • Tanaka I., Kurihara K., Chatake T., and Niimura N. A high-performance neutron diffractometer for biological crystallography (BIX-3). J. Appl. Crystallogr. 35 (2002) 34-40
    • (2002) J. Appl. Crystallogr. , vol.35 , pp. 34-40
    • Tanaka, I.1    Kurihara, K.2    Chatake, T.3    Niimura, N.4
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 18
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. Struct. J. Biol. 125 (1999) 156-165
    • (1999) Struct. J. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 19
    • 0346122798 scopus 로고    scopus 로고
    • GRASP2: visualization, surface properties, and electrostatics of macromolecular structures and sequences
    • Petrey D., and Honig B. GRASP2: visualization, surface properties, and electrostatics of macromolecular structures and sequences. Methods Enzymol. 374 (2003) 492-509
    • (2003) Methods Enzymol. , vol.374 , pp. 492-509
    • Petrey, D.1    Honig, B.2
  • 20
    • 0037391226 scopus 로고    scopus 로고
    • Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding
    • Diao J. Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding. Acta Crystallogr. D59 (2003) 670-676
    • (2003) Acta Crystallogr. , vol.D59 , pp. 670-676
    • Diao, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.