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Volumn 79, Issue 6, 2000, Pages 3139-3143

Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; GLYCINE; ION CHANNEL; MEMBRANE PROTEIN; PROTON;

EID: 0033636640     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76547-7     Document Type: Article
Times cited : (47)

References (12)
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  • 3
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    • Vibrational analysis of peptides, polypeptides and proteins. XV. Crystalline polyglycine II
    • Dwivedi, A., and S. Krimm. 1982. Vibrational analysis of peptides, polypeptides and proteins. XV. Crystalline polyglycine II. Biopolymers. 21:2377-2397.
    • (1982) Biopolymers , vol.21 , pp. 2377-2397
    • Dwivedi, A.1    Krimm, S.2
  • 6
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: A method for resolving intrinsically overlapped bands
    • Kauppinen, J., D. Moffatt, H. Mantsch, and D. Cameron. 1982. Fourier self-deconvolution: a method for resolving intrinsically overlapped bands. Appl Spectrosc. 35:271-276.
    • (1982) Appl Spectrosc. , vol.35 , pp. 271-276
    • Kauppinen, J.1    Moffatt, D.2    Mantsch, H.3    Cameron, D.4
  • 7
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane four-helix bundle of influenza a M2 protein channel: Structural implications from helix tilt and orientation
    • Kovacs, F., and T. Cross. 1997. Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation. Biophys. J. 73:2511-2517.
    • (1997) Biophys. J. , vol.73 , pp. 2511-2517
    • Kovacs, F.1    Cross, T.2
  • 8
    • 0033605318 scopus 로고    scopus 로고
    • Experimentally based orientational refinement of membrane proteins: A structure for the influenza a M2 H+ channel
    • Kukol, A., P. Adams, L. Rice, A. Brunger, and I. Arkin. 1999. Experimentally based orientational refinement of membrane proteins: a structure for the influenza A M2 H+ channel. J. Mol. Biol. 286:951-962.
    • (1999) J. Mol. Biol. , vol.286 , pp. 951-962
    • Kukol, A.1    Adams, P.2    Rice, L.3    Brunger, A.4    Arkin, I.5
  • 9
    • 0032819359 scopus 로고    scopus 로고
    • Vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching
    • Kukol, A., and I. Arkin. 1999a. Vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching. Biophys. J. 77:1594-1601.
    • (1999) Biophys. J. , vol.77 , pp. 1594-1601
    • Kukol, A.1    Arkin, I.2
  • 10
    • 0034635424 scopus 로고    scopus 로고
    • Structure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching
    • Kukol, A., and I. Arkin. 2000. Structure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching. J. Biol. Chem. 275: 4225-4229.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4225-4229
    • Kukol, A.1    Arkin, I.2
  • 11
    • 84984086749 scopus 로고
    • Infrared spectra of isotopic polyglycines
    • Suzuki, S., Y. Iwashita, and T. Shimanouchi. 1966. Infrared spectra of isotopic polyglycines. Biopolymers. 4:337-350.
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  • 12
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    • Infrared dichroism and molecular conformation of α-form poly-g-benzyl-L-glutamate
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.