Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency Export

@article{citeulike:3956140, abstract = {The phenomena of protein reconstitution and three-dimensional domain swapping reveal that highly similar structures can be obtained whether a protein is comprised of one or more polypeptide chains. In this review, we use protein reconstitution as a lens through which to examine the range of protein tolerance to chain interruptions and the roles of the primary structure in related features of protein structure and folding, including circular permutation, natively unfolded proteins, allostery, and amyloid fibril formation. The results imply that noncovalent interactions in a protein are sufficient to specify its structure under the constraints imposed by the covalent backbone.}, address = {Chemistry Department, Princeton University, Princeton, New Jersey, 08544-1009 USA; Department of Biophysical Chemistry, Chemical Center, Lund University, S22100 Lund, Sweden}, author = {Carey, Jannette and Lindman, Stina and Bauer, Mikael and Linse, Sara}, citeulike-article-id = {3956140}, citeulike-linkout-0 = {http://dx.doi.org/10.1110/ps.072985007}, citeulike-linkout-1 = {http://www3.interscience.wiley.com/cgi-bin/abstract/121603259/ABSTRACT}, doi = {10.1110/ps.072985007}, journal = {Protein Science}, keywords = {domain\_swapping, oligomer, protein, review}, number = {11}, pages = {2317--2333}, posted-at = {2009-01-27 07:30:37}, priority = {2}, title = {Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency}, url = {http://dx.doi.org/10.1110/ps.072985007}, volume = {16}, year = {2007} }

TY - JOUR ID - citeulike:3956140 L3 - citeulike-article-id:3956140 N2 - The phenomena of protein reconstitution and three-dimensional domain swapping reveal that highly similar structures can be obtained whether a protein is comprised of one or more polypeptide chains. In this review, we use protein reconstitution as a lens through which to examine the range of protein tolerance to chain interruptions and the roles of the primary structure in related features of protein structure and folding, including circular permutation, natively unfolded proteins, allostery, and amyloid fibril formation. The results imply that noncovalent interactions in a protein are sufficient to specify its structure under the constraints imposed by the covalent backbone. IS - 11 JF - Protein Science AD - Chemistry Department, Princeton University, Princeton, New Jersey, 08544-1009 USA; Department of Biophysical Chemistry, Chemical Center, Lund University, S22100 Lund, Sweden EP - 2333 TI - Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency VL - 16 SP - 2317 KW - domain_swapping KW - oligomer KW - protein KW - review AU - Carey, Jannette AU - Lindman, Stina AU - Bauer, Mikael AU - Linse, Sara PY - 2007/// UR - http://dx.doi.org/10.1110/ps.072985007 ER -