skip to main content
Ngôn ngữ:
Giới hạn tìm kiếm: Giới hạn tìm kiếm: Dạng tài nguyên Hiển thị kết quả với: Hiển thị kết quả với: Chỉ mục

Folding of a large protein at high structural resolution.(BIOPHYSICS AND COMPUTATIONAL BIOLOGY)(Report)(Author abstract)

Walters, Benjamin T. ; Mayne, Leland ; Hinshaw, James R. ; Sosnick, Tobin R. ; Englander, S. Walter

Proceedings of the National Academy of Sciences of the United States, Nov 19, 2013, Vol.110(47), p.18898(6) [Tạp chí có phản biện]

ISSN: 0027-8424

Toàn văn sẵn có

Trích dẫn Trích dẫn bởi
  • Nhan đề:
    Folding of a large protein at high structural resolution.(BIOPHYSICS AND COMPUTATIONAL BIOLOGY)(Report)(Author abstract)
  • Tác giả: Walters, Benjamin T. ; Mayne, Leland ; Hinshaw, James R. ; Sosnick, Tobin R. ; Englander, S. Walter
  • Chủ đề: Protein Folding -- Research ; Protein Structure -- Research
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States, Nov 19, 2013, Vol.110(47), p.18898(6)
  • Mô tả: Kinetic folding of the large two-domain maltose binding protein (MBP; 370 residues) was studied at high structural resolution by an advanced hydrogen-exchange pulse-labeling mass-spectrometry method (HX MS). Dilution into folding conditions initiates a fast molecular collapse into a polyglobular conformation (<20 ms), determined by various methods including small angle X-ray scattering. The compaction produces a structurally heterogeneous state with widespread low-level HX protection and spectroscopic signals that match the equilibrium melting posttransition-state baseline. In a much slower step (7-s time constant), all of the MBP molecules, although initially heterogeneously structured, form the same distinct helix plus sheet folding intermediate with the same time constant. The intermediate is composed of segments that are distant in the MBP sequence but adjacent in the native protein where they close the longest residue-to-residue contact. Segments that are most HX protected in the early molecular collapse do not contribute to the initial intermediate, whereas the segments that do participate are among the less protected. The 7-s intermediate persists through the rest of the folding process. It contains the sites of three previously reported destabilizing mutations that greatly slow folding. These results indicate that the intermediate is an obligatory step on the MBP folding pathway. MBP then folds to the native state on a longer time scale (~100 s), suggestively in more than one step, the first of which forms structure adjacent to the 7-s intermediate. These results add a large protein to the list of proteins known to fold through distinct native-like intermediates in distinct pathways. SAXS | HDX | protein collapse | denatured state ensemble www.pnas.org/cgi/doi/ 10.1073/pnas.1319482110
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424

Đang tìm Cơ sở dữ liệu bên ngoài...