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

Journal Article · Tue Aug 14 00:00:00 EDT 1990 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00484a007· OSTI ID:5935281

Eberle, W ^[1]; Klaus, W ^[2]; Cesareni, G ^[3]; Sander, C ^[4]; Roesch, P ^[3]

---

1. Max-Planck-Institute for Medical Research, Heidelberg (West Germany) European Molecular Biology Lab., Heidelberg (West Germany)
2. Gesellschaft fuer Biotechnologische Forschung, Braunschweig (West Germany)
3. Max-Planck-Institute for Medical Research, Heidelberg (West Germany)
4. European Molecular Biology Lab., Heidelberg (West Germany)

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 ({sup 1}H 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 {sup 3}J{sub HN{alpha}} 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.

• OSTI ID: 5935281
• Journal Information: Biochemistry; (USA), Vol. 29:32; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
GENE REPRESSORS
MOLECULAR STRUCTURE
NUCLEOPROTEINS
NUCLEAR MAGNETIC RESONANCE
CHEMICAL SHIFT
HEAVY WATER
OVERHAUSER EFFECT
PROTONS
BARYONS
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HYDROGEN COMPOUNDS
MAGNETIC RESONANCE
NUCLEONS
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PROTEINS
RESONANCE
WATER
550601* - Medicine- Unsealed Radionuclides in Diagnostics