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Literature DB >> 1056017

Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.

P J Cozzone, S J Opella, O Jardetzky, J Berthou, P Jollès.

Abstract

A specific temperature-dependent conformational transition of hen egg-white lysozyme, occurring between 20 degree C and 30 degree C in solution, has been detected by 13-C-nuclear magnetic resonance spectroscopy. Selective changes in the chemical shifts of aromatic residues, together with differences in the chemical shifts, and nuclear Overhauser enhancement in the carbonyl, carboxyl, and alpha-carbon regions of the spectrum point to the vicinity of subsites D and E as the primary locus of the structural change.

Entities: Chemical

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Year: 1975 PMID： 1056017 PMCID： PMC432702 DOI： 10.1073/pnas.72.6.2095

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

14 in total

1. THERMODYNAMICS OF CONFORMATIONAL CHANGES OF PROTEINS. I. PH-DEPENDENT DENATURATION OF MURAMIDASE.

Authors: A J SOPHIANOPOULOS; B J WEISS
Journal: Biochemistry Date: 1964-12 Impact factor: 3.162

2. Carbon-13 Fourier transform NMR studies in 20 mm sample tubes: observation of individual carbon sites in proteins.

Authors: A Allerhand; R F Childers; E Oldfield
Journal: Ann N Y Acad Sci Date: 1973-12-31 Impact factor: 5.691

3. On the conformation of the hen egg-white lysozyme molecule.

Authors: C C Blake; G A Mair; A C North; D C Phillips; V R Sarma
Journal: Proc R Soc Lond B Biol Sci Date: 1967-04-18

4. Letter: Carbon magnetic resonance study of the conformational changes in carp muscle calcium binding parvalbumin.

Authors: S J Opella; D J Nelson; O Jardetzyk
Journal: J Am Chem Soc Date: 1974-10-30 Impact factor: 15.419

5. Fluctuation of the lysozyme structure. II. Effects of temperature and binding of inhibitors.

Authors: M Nakanishi; M Tsuboi; A Ikegami
Journal: J Mol Biol Date: 1973-04-25 Impact factor: 5.469

6. Natrual-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Observation of numerous single-carbon resonances of hen egg-white lysozyme.

Authors: A Allerhand; R F Childers; E Oldfield
Journal: Biochemistry Date: 1973-03-27 Impact factor: 3.162

4. The temperature and pH-dependent transition of hen lysozyme. Characterization of two temperature-defined domains and of an N-acetylglucosamine (inhibitor)-insensitive form.

Authors: J Saint-Blancard; J Mazurier; M Bournaud; J P Maurel; J Berthou; P Jollès
Journal: Mol Biol Rep Date: 1979-08-31 Impact factor: 2.316

4 in total

Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.

1. THERMODYNAMICS OF CONFORMATIONAL CHANGES OF PROTEINS. I. PH-DEPENDENT DENATURATION OF MURAMIDASE.

2. Carbon-13 Fourier transform NMR studies in 20 mm sample tubes: observation of individual carbon sites in proteins.

3. On the conformation of the hen egg-white lysozyme molecule.

4. Letter: Carbon magnetic resonance study of the conformational changes in carp muscle calcium binding parvalbumin.

5. Fluctuation of the lysozyme structure. II. Effects of temperature and binding of inhibitors.

6. Natrual-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Observation of numerous single-carbon resonances of hen egg-white lysozyme.

7. Preliminary x-ray investigation of duck egg-white lysozyme II.

8. Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozyme.

9. Carbon-13 Fourier transform nuclear magnetic resonance. II. Ribonuclease.

10. Crystallization of a multienzyme complex: fatty acid synthetase from yeast.

1. Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules.

Review 2. What's new in lysozyme research? Always a model system, today as yesterday.

3. Proton magnetic resonance spectroscopic studies of proteins containing deuterated tryptophan residues.

4. The temperature and pH-dependent transition of hen lysozyme. Characterization of two temperature-defined domains and of an N-acetylglucosamine (inhibitor)-insensitive form.