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Literature DB >> 10625416

May the driving force be with you--whatever it is.

Abstract

Changes in the atomic coordinate fluctuations contribute to the entropy of biomolecular processes such as complex formation. Characterizations of such changes in proteins reveal that the response may be dramatically different between the backbone and the side chains, and further resolve enthalpy-entropy compensation at the molecular level.

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Year: 2000 PMID： 10625416 DOI： 10.1038/71202

Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368

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Cited

11 in total

1. Short constrained peptides that inhibit HIV-1 entry.

Authors: Samuel K Sia; Peter A Carr; Andrea G Cochran; Vladimir N Malashkevich; Peter S Kim
Journal: Proc Natl Acad Sci U S A Date: 2002-11-04 Impact factor: 11.205

2. Analysis of side chain mobility among protein G B1 domain mutants with widely varying stabilities.

Authors: Virginia A Goehlert; Ewa Krupinska; Lynne Regan; Martin J Stone
Journal: Protein Sci Date: 2004-11-10 Impact factor: 6.725

3. Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain.

Authors: Liliya Vugmeyster; Dmitry Ostrovsky
Journal: J Biomol NMR Date: 2011-03-17 Impact factor: 2.835

4. Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods.

Authors: Angeles Canales-Mayordomo; Rosa Fayos; Jesús Angulo; Rafael Ojeda; Manuel Martín-Pastor; Pedro M Nieto; Manuel Martín-Lomas; Rosa Lozano; Guillermo Giménez-Gallego; Jesús Jiménez-Barbero
Journal: J Biomol NMR Date: 2006-07-29 Impact factor: 2.835

May the driving force be with you--whatever it is.

1. Short constrained peptides that inhibit HIV-1 entry.

2. Analysis of side chain mobility among protein G B1 domain mutants with widely varying stabilities.

3. Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain.

4. Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods.

5. The HoxB1 hexapeptide is a prefolded domain: implications for the Pbx1/Hox interaction.

6. Dynamic activation of an allosteric regulatory protein.

7. Ultrafast NMR T1 relaxation measurements: probing molecular properties in real time.

8. Dynamically driven protein allostery.

9. Using metadynamics to understand the mechanism of calmodulin/target recognition at atomic detail.

10. The HAB1 PP2C is inhibited by ABA-dependent PYL10 interaction.