Abstract
Antiserum to bovine serum albumin was fractionated into populations of antibody directed against party, an apparent pathway of refolding within each domain was obtained which is consistent with the proposed evolutionary pathway of the albumin molecule. The COOH-terminal one-third of each domain refolds faster than the NH2-terminal two-thirds of each respective domain. In addition, further evidence in given for a correlation between the rate of refolding and the degree of interdomain influence that might restrict refolding.
Highlights
Antiserum to bovine serum albumin was fractionated into populations of antibody directed against particular areas of the albumin molecule
Additional restricted populations of antibody refolding were obtained in order to examine the pathway of within each domain of the molecule. These results demonstrated that the last disulfide-bonded double loop in each of the three domains refolded more rapidly than each of the three respective domains
It has been proposed that the albumin molecule consists of three domains of equivalent size [12]
Summary
Antiserum to bovine serum albumin was fractionated into populations of antibody directed against particular areas of the albumin molecule Using these fractionated populations of antibody, an apparent pathway of refolding within each domain was obtained which is consistent with the proposed evolutionary pathway of the albumin molecule. (3) proposed that even a small protein would not be able to thermodynamically search all possible conformations within such a short time. He suggested a kinetic control that would limit the number of available pathways. Is especially attractive as a means of limiting the number of available pathways This model states that a short sequence of amino acids within the molecule folds preferentially into a small number of conformational states that will form or be part of metastable intermediates. Evidence for the existence of folding intermediates has been provided by several investigators including Creighton
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