Water mediation in protein folding and molecular recognition.

@article{citeulike:749842, abstract = {Water is essential for life in many ways, and without it biomolecules might no longer truly be biomolecules. In particular, water is important to the structure, stability, dynamics, and function of biological macromolecules. In protein folding, water mediates the collapse of the chain and the search for the native topology through a funneled energy landscape. Water actively participates in molecular recognition by mediating the interactions between binding partners and contributes to either enthalpic or entropic stabilization. Accordingly, water must be included in recognition and structure prediction codes to capture specificity. Thus water should not be treated as an inert environment, but rather as an integral and active component of biomolecular systems, where it has both dynamic and structural roles. Focusing on water sheds light on the physics and function of biological machinery and self-assembly and may advance our understanding of the natural design of proteins and nucleic acids.}, address = {Center for Theoretical Biological Physics and Department of Physics, University of California at San Diego, La Jolla, California 92093, USA.}, author = {Levy, Y. and Onuchic, J. N. }, citeulike-article-id = {749842}, doi = {10.1146/annurev.biophys.35.040405.102134}, issn = {1056-8700}, journal = {Annu Rev Biophys Biomol Struct}, pages = {389--415}, posted-at = {2008-07-30 18:01:28}, priority = {2}, title = {Water mediation in protein folding and molecular recognition.}, url = {http://dx.doi.org/10.1146/annurev.biophys.35.040405.102134}, volume = {35}, year = {2006} }

TY - JOUR ID - citeulike:749842 L3 - citeulike-article-id:749842 TI - Water mediation in protein folding and molecular recognition. JF - Annu Rev Biophys Biomol Struct VL - 35 SP - 389 EP - 415 AD - Center for Theoretical Biological Physics and Department of Physics, University of California at San Diego, La Jolla, California 92093, USA. SN - 1056-8700 N2 - Water is essential for life in many ways, and without it biomolecules might no longer truly be biomolecules. In particular, water is important to the structure, stability, dynamics, and function of biological macromolecules. In protein folding, water mediates the collapse of the chain and the search for the native topology through a funneled energy landscape. Water actively participates in molecular recognition by mediating the interactions between binding partners and contributes to either enthalpic or entropic stabilization. Accordingly, water must be included in recognition and structure prediction codes to capture specificity. Thus water should not be treated as an inert environment, but rather as an integral and active component of biomolecular systems, where it has both dynamic and structural roles. Focusing on water sheds light on the physics and function of biological machinery and self-assembly and may advance our understanding of the natural design of proteins and nucleic acids. AU - Levy, Y AU - Onuchic, JN PY - 2006/// UR - http://dx.doi.org/10.1146/annurev.biophys.35.040405.102134 ER -