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Literature DB >> 8057864

Structure and energy change in hemoglobin by hydrogen exchange labeling.

S W Englander¹, J J Englander.

Abstract

Entities: Chemical

Mesh：

Substances：

Year: 1994 PMID： 8057864 DOI： 10.1016/0076-6879(94)32041-1

Source DB: PubMed Journal: Methods Enzymol ISSN： 0076-6879 Impact factor: 1.600

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11 in total

1. Backbone resonance assignments of human adult hemoglobin in the carbonmonoxy form.

Authors: Jonathan A Lukin; Georg Kontaxis; Virgil Simplaceanu; Yue Yuan; Ad Bax; Chien Ho
Journal: J Biomol NMR Date: 2004-02 Impact factor: 2.835

2. Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS.

Authors: Dennis Pantazatos; Jack S Kim; Heath E Klock; Raymond C Stevens; Ian A Wilson; Scott A Lesley; Virgil L Woods
Journal: Proc Natl Acad Sci U S A Date: 2004-01-08 Impact factor: 11.205

3. Truncated human serum albumin retains general anaesthetic binding activity.

Authors: Renyu Liu; Jinsheng Yang; Chung-Eun Ha; Nadhipuram V Bhagavan; Roderic G Eckenhoff
Journal: Biochem J Date: 2005-05-15 Impact factor: 3.857

Review 4. Hydrogen exchange and mass spectrometry: A historical perspective.

Authors: S Walter Englander
Journal: J Am Soc Mass Spectrom Date: 2006-07-28 Impact factor: 3.109

5. Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry.

Authors: Marc L Mendillo; Christopher D Putnam; Ashley O Mo; Jonathan W Jamison; Sheng Li; Virgil L Woods; Richard D Kolodner
Journal: J Biol Chem Date: 2010-02-24 Impact factor: 5.157

Structure and energy change in hemoglobin by hydrogen exchange labeling.

1. Backbone resonance assignments of human adult hemoglobin in the carbonmonoxy form.

2. Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS.

3. Truncated human serum albumin retains general anaesthetic binding activity.

Review 4. Hydrogen exchange and mass spectrometry: A historical perspective.

5. Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry.

Review 6. Mechanisms and uses of hydrogen exchange.

7. Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain.

8. Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry.

9. Comparative binding character of two general anaesthetics for sites on human serum albumin.

10. Differential halothane binding and effects on serum albumin and myoglobin.