Energy Landscape and Dynamics of Biomolecules Extended Abstract

Author： Frauenfelder Hans  

Publisher： Springer Publishing Company

ISSN： 0092-0606

Source： Journal of Biological Physics, Vol.31, Iss.3-4, 2005-12, pp. : 413-416

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Proteins are not isolated homogeneous systems. Each protein can exist in a very large number of conformations (conformational substates) that are characterized by an energy landscape. The main conformational motions, similar to the α and β fluctuations in glasses, are linked to fluctuations in the bulk solvent and the hydration shell.

Related content

Extended Abstract: Plateaus and Jumps in Single-Molecule DNA Unzipping Experiments

By Nelson David  

Journal of Biological Physics, Vol. 31, Iss. 3-4, 2005-12 ,pp. : 241-242 (2)

Springer Publishing Company

Access to resources Recommend Favorite

Role of methyl groups in dynamics and evolution of biomolecules

By Nickels Jonathan  

Journal of Biological Physics, Vol. 38, Iss. 3, 2012-06 ,pp. : 497-505 (9)

Springer Publishing Company

Access to resources Recommend Favorite

Conformational equilibria and dynamics of cytochrome c induced by binding of sodium dodecyl sulfate monomers and micelles

By Oellerich Silke   Wackerbarth Hainer   Hildebrandt Peter  

European Biophysics Journal, Vol. 32, Iss. 7, 2004-11 ,pp. : 599-613 (15)

Springer Publishing Company

Access to resources Recommend Favorite

Free energies of binding of R- and S-propranolol to wild-type and F483A mutant cytochrome P450 2D6 from molecular dynamics simulations

By Graaf Chris   Oostenbrink Chris   Keizers Peter   Vugt-Lussenburg Barbara   Commandeur Jan   Vermeulen Nico  

European Biophysics Journal, Vol. 36, Iss. 6, 2007-07 ,pp. : 589-599 (11)

Springer Publishing Company

Access to resources Recommend Favorite

Changes in the level of poly(Phe) synthesis in Escherichia coli ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus can be explained by structural changes in the peptidyltransferase center: a molecular dynamics simulation analysis

By Papadopoulos G.   Grudinin S.   Kalpaxis D.   Choli-Papadopoulou T.  

European Biophysics Journal, Vol. 35, Iss. 8, 2006-10 ,pp. : 675-683 (9)

Springer Publishing Company

Access to resources Recommend Favorite