Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein

W. Eberle; W. Klaus; G. Cesareni; C. Sander; P. Rosch

doi:10.1021/bi00484a007

Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein

W. Eberle, W. Klaus, G. Cesareni, C. Sander, P. Rosch

Fondazione Santa Lucia

Research output: Contribution to journal › Article

Abstract

The complete resonance assignment of the Co1E1 rop (rom) protein at pH 2.3 was obtained by two-dimensional (2D) proton nuclear magnetic resonance spectroscopy (¹H NMR) at 500 and 600 MHz using through-bond and through-space connectivities. Sequential assignments and elements of regular secondary structure were deduced by analysis of nuclear Overhauser enhancement spectroscopy (NOESY) experiments and ³J(HNα) coupling constants. One 7.2-kDa monomer of the homodimer consists of two antiparallel helices connected by a hairpin loop at residue 31. The C-terminal peptide consisting of amino acids 59-63 shows no stable conformation. The dimer forms a four-helix bundle with opposite polarization of neighboring elements in agreement with the X-ray structure.

Original language	English
Pages (from-to)	7402-7407
Number of pages	6
Journal	Biochemistry
Volume	29
Issue number	32
DOIs	https://doi.org/10.1021/bi00484a007
Publication status	Published - 1990

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1021/bi00484a007

Fingerprint Dive into the research topics of 'Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein'. Together they form a unique fingerprint.

Cite this

Eberle, W., Klaus, W., Cesareni, G., Sander, C., & Rosch, P. (1990). Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein. Biochemistry, 29(32), 7402-7407. https://doi.org/10.1021/bi00484a007

@article{e0edbd71a3f74f8fb9902d7bf42cd2ed,

title = "Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein",

abstract = "The complete resonance assignment of the Co1E1 rop (rom) protein at pH 2.3 was obtained by two-dimensional (2D) proton nuclear magnetic resonance spectroscopy (1H NMR) at 500 and 600 MHz using through-bond and through-space connectivities. Sequential assignments and elements of regular secondary structure were deduced by analysis of nuclear Overhauser enhancement spectroscopy (NOESY) experiments and 3J(HNα) coupling constants. One 7.2-kDa monomer of the homodimer consists of two antiparallel helices connected by a hairpin loop at residue 31. The C-terminal peptide consisting of amino acids 59-63 shows no stable conformation. The dimer forms a four-helix bundle with opposite polarization of neighboring elements in agreement with the X-ray structure.",

author = "W. Eberle and W. Klaus and G. Cesareni and C. Sander and P. Rosch",

year = "1990",

doi = "10.1021/bi00484a007",

language = "English",

volume = "29",

pages = "7402--7407",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "32",

}

TY - JOUR

T1 - Proton nuclear magnetic resonance assignments and secondary structure determination of the Co1E1 rop (rom) protein

AU - Eberle, W.

AU - Klaus, W.

AU - Cesareni, G.

AU - Sander, C.

AU - Rosch, P.

PY - 1990

Y1 - 1990

N2 - The complete resonance assignment of the Co1E1 rop (rom) protein at pH 2.3 was obtained by two-dimensional (2D) proton nuclear magnetic resonance spectroscopy (1H NMR) at 500 and 600 MHz using through-bond and through-space connectivities. Sequential assignments and elements of regular secondary structure were deduced by analysis of nuclear Overhauser enhancement spectroscopy (NOESY) experiments and 3J(HNα) coupling constants. One 7.2-kDa monomer of the homodimer consists of two antiparallel helices connected by a hairpin loop at residue 31. The C-terminal peptide consisting of amino acids 59-63 shows no stable conformation. The dimer forms a four-helix bundle with opposite polarization of neighboring elements in agreement with the X-ray structure.

AB - The complete resonance assignment of the Co1E1 rop (rom) protein at pH 2.3 was obtained by two-dimensional (2D) proton nuclear magnetic resonance spectroscopy (1H NMR) at 500 and 600 MHz using through-bond and through-space connectivities. Sequential assignments and elements of regular secondary structure were deduced by analysis of nuclear Overhauser enhancement spectroscopy (NOESY) experiments and 3J(HNα) coupling constants. One 7.2-kDa monomer of the homodimer consists of two antiparallel helices connected by a hairpin loop at residue 31. The C-terminal peptide consisting of amino acids 59-63 shows no stable conformation. The dimer forms a four-helix bundle with opposite polarization of neighboring elements in agreement with the X-ray structure.

UR - http://www.scopus.com/inward/record.url?scp=0024997234&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024997234&partnerID=8YFLogxK

U2 - 10.1021/bi00484a007

DO - 10.1021/bi00484a007

M3 - Article

C2 - 2223771

AN - SCOPUS:0024997234

VL - 29

SP - 7402

EP - 7407

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 32

ER -