منابع مشابه
The radius of gyration of an apomyoglobin folding intermediate.
Sph site of pSL301 (Invitrogen). Colonies were screened for inserts by PCR with T7 and T3 sequences located outside the cloning site as primers. 10. Selected clones were manually sequenced as described [G. (1989)] with 5'-GACGTCGAC-CTGAGGTAATTATAACC-3' as primer. Sequence files were analyzed by means of the SAGE software group (7), which identifies the anchoring enzyme site with the proper spac...
متن کاملDetermine folding mechanism of Lali structure, northern Dezful, Zagros, Iran
Lali sub-surface structure, with a NW-SE Zagros trending is located in Dezful Embayment. To determine the folding mechanism, structural geometric parameters including limbs dip, amplitude, wavelength, and crestal length were determined in four stages during deformation. In order to investigate the lateral folding mechanism, these geometric parameters were analyzed in three parts in the Lal...
متن کاملThe pKa of His-24 in the folding transition state of apomyoglobin.
In native apomyoglobin, His-24 cannot be protonated, although at pH 4 the native protein forms a molten globule folding intermediate in which the histidine residues are readily protonated. The inability to protonate His-24 in the native protein dramatically affects the unfolding/refolding kinetics, as demonstrated by simulations for a simple model. Kinetic data for wild type and for a mutant la...
متن کاملStructure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.
Apomyoglobin folding proceeds through a molten globule intermediate (low-salt form; I1) that has been characterized by equilibrium (pH 4) and kinetic (pH 6) folding experiments. Of the eight alpha-helices in myoglobin, three (A, G, and H) are structured in I1, while the rest appear to be unfolded. Here we report on the structure and stability of a second intermediate, the trichloroacetate form ...
متن کاملDirect observation of fast protein folding: the initial collapse of apomyoglobin.
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of ste...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2020
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.60.215