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Protein dynamics simulations from nanoseconds to microseconds
- Source :
- Current Opinion in Structural Biology. 9:157-163
- Publication Year :
- 1999
- Publisher :
- Elsevier BV, 1999.
-
Abstract
- There have been a number of advances in atomic resolution simulations of biomolecules during the past few years. These have arisen partly from improvements to computer power and partly from algorithmic improvements. There have also been advances in measuring time-dependent fluctuations in proteins using NMR spectroscopy, revealing the importance of fluctuations in the microsecond to millisecond time range. Progress has also been made in measuring how far the simulations are able to represent the accessible phase space that is available to the protein in its native state, in solution, at room temperature. Another area of development is the simulation of protein unfolding at atomic resolution.
- Subjects :
- Models, Molecular
Protein Denaturation
Protein Folding
Millisecond
Magnetic Resonance Spectroscopy
Protein Conformation
Chemistry
Protein dynamics
Proteins
Nanosecond
Computational physics
Microsecond
Structural Biology
Atomic resolution
Phase space
Biophysics
Thermodynamics
Molecular Biology
Time range
Algorithms
Subjects
Details
- ISSN :
- 0959440X
- Volume :
- 9
- Database :
- OpenAIRE
- Journal :
- Current Opinion in Structural Biology
- Accession number :
- edsair.doi.dedup.....908253fbac0e2ac6fa162d9283b55d44
- Full Text :
- https://doi.org/10.1016/s0959-440x(99)80022-0