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1.

Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.
by Liang, Fu-Cheng

Proceedings of the National Academy of Sciences of the United States of America, March 22, 2016, Vol.113(12), pp.E1615-E1624

2.

Kinetic analysis of the multistep aggregation pathway of human transthyretin.
by Sun, Xun

Proceedings of the National Academy of Sciences of the United States of America, July 3, 2018, Vol.115(27), pp.E6201-E6208

3.

Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.
by Uzawa, Takanori

Proceedings of the National Academy of Sciences of the United States of America, September 16, 2008, Vol.105(37), pp.13859-13864

4.

Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.
by Nishimura, Chiaki

Proceedings of the National Academy of Sciences of the United States of America, March 29, 2005, Vol.102(13), pp.4765-4770

5.

Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands.
by Boehr, David D

Proceedings of the National Academy of Sciences of the United States of America, January 26, 2010, Vol.107(4), pp.1373-1378

6.

Molecular basis for modulation of biological function by alternate splicing of the Wilms' tumor suppressor protein.
by Laity, J H

Proceedings of the National Academy of Sciences of the United States of America, October 24, 2000, Vol.97(22), pp.11932-11935

7.

Two different neurodegenerative diseases caused by proteins with similar structures.
by Mo, H

Proceedings of the National Academy of Sciences of the United States of America, February 27, 2001, Vol.98(5), pp.2352-2357

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