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Literature DB >> 9615171

Deciphering the molecular code of hemoglobin allostery.

G K Ackers¹.

Abstract

Mesh：

Substances：
Hemoglobins

Year: 1998 PMID： 9615171 DOI： 10.1016/s0065-3233(08)60653-1

Source DB: PubMed Journal: Adv Protein Chem ISSN： 0065-3233

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28 in total

1. Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble.

Authors: H Pan; J C Lee; V J Hilser
Journal: Proc Natl Acad Sci U S A Date: 2000-10-24 Impact factor: 11.205

2. Energetics by NMR: site-specific binding in a positively cooperative system.

Authors: Gregory P Tochtrop; Klaus Richter; Changguo Tang; James J Toner; Douglas F Covey; David P Cistola
Journal: Proc Natl Acad Sci U S A Date: 2002-02-19 Impact factor: 11.205

3. Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function.

Authors: Gary K Ackers; Paula M Dalessio; George H Lew; Margaret A Daugherty; Jo M Holt
Journal: Proc Natl Acad Sci U S A Date: 2002-07-15 Impact factor: 11.205

4. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.

Authors: Cristiano Viappiani; Stefano Bettati; Stefano Bruno; Luca Ronda; Stefania Abbruzzetti; Andrea Mozzarelli; William A Eaton
Journal: Proc Natl Acad Sci U S A Date: 2004-09-22 Impact factor: 11.205

5. An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate.

Authors: Yue Yuan; Virgil Simplaceanu; Nancy T Ho; Chien Ho
Journal: Biochemistry Date: 2010-11-29 Impact factor: 3.162

6. Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

Authors: Steven T Whitten; Bertrand García-Moreno E; Vincent J Hilser
Journal: Proc Natl Acad Sci U S A Date: 2005-03-14 Impact factor: 11.205

Deciphering the molecular code of hemoglobin allostery.

1. Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble.

2. Energetics by NMR: site-specific binding in a positively cooperative system.

3. Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function.

4. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.

5. An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate.

6. Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

7. Acid destabilization of the solution conformation of Bcl-xL does not drive its pH-dependent insertion into membranes.

8. Coarse-grained free energy functions for studying protein conformational changes: a double-well network model.

Review 9. Protein dynamics explain the allosteric behaviors of hemoglobin.

10. Allostery turns 50: is the vintage yet attractive?