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Literature DB >> 1631313

Investigation of higher order structures of proteins by ultraviolet resonance Raman spectroscopy.

Abstract

Progress in laser technology and light detection devices have enabled us to explore protein structures and their dynamics by using time-resolved resonance Raman spectroscopy. It is in the last decade that Raman spectra of proteins excited at 200-240 nm have brought about rich structural information. The technological developments in deep UV resonance Raman spectroscopy are reviewed first, and the unique information on proteins obtainable from such spectra are summarized. As an application of this technique to investigations of the higher order structures of proteins, studies on the quaternary structure transition of haemoglobin are described.

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Year: 1992 PMID： 1631313 DOI： 10.1016/0079-6107(92)90009-u

Source DB: PubMed Journal: Prog Biophys Mol Biol ISSN： 0079-6107 Impact factor: 3.667

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Cited

8 in total

1. Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation.

Authors: Uri Samuni; Camille J Roche; David Dantsker; Laura J Juszczak; Joel M Friedman
Journal: Biochemistry Date: 2006-03-07 Impact factor: 3.162

2. Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.

Authors: Eric M Jones; Gurusamy Balakrishnan; Thomas G Spiro
Journal: J Am Chem Soc Date: 2012-02-09 Impact factor: 15.419

3. Functional consequences of mutations at the allosteric interface in hetero- and homo-hemoglobin tetramers.

Authors: V Baudin; J Pagnier; L Kiger; J Kister; O Schaad; M T Bihoreau; N Lacaze; M C Marden; S J Edelstein; C Poyart
Journal: Protein Sci Date: 1993-08 Impact factor: 6.725

4. His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.

Authors: Gurusamy Balakrishnan; Ying Hu; Thomas G Spiro
Journal: J Am Chem Soc Date: 2012-11-06 Impact factor: 15.419

5. Normal coordinate structural decomposition of the heme distortions of hemoglobin in various quaternary states and bound to allosteric effectors.

Authors: Monique Laberge; Takashi Yonetani; Judit Fidy
Journal: Mol Divers Date: 2003 Impact factor: 2.943

Investigation of higher order structures of proteins by ultraviolet resonance Raman spectroscopy.

1. Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation.

2. Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.

3. Functional consequences of mutations at the allosteric interface in hetero- and homo-hemoglobin tetramers.

4. His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.

5. Normal coordinate structural decomposition of the heme distortions of hemoglobin in various quaternary states and bound to allosteric effectors.

6. Label-Free SERS Detection of Small Proteins Modified to Act as Bifunctional Linkers.

Review 7. Protein dynamics from time resolved UV Raman spectroscopy.

8. Primary protein response after ligand photodissociation in carbonmonoxy myoglobin.