By Lathrop R. H., Rogers Jr R. G., Smith T. F.
A rigorous Bayesian research is gifted that unifies protein sequence-structure alignment and popularity. Given a chain, particular formulae are derived to choose (1) its globally so much possible center constitution from a constitution library; (2) its globally such a lot possible alignment to a given center constitution; (3) its so much possible joint middle constitution and alignment selected globally around the complete library; and (4) its such a lot possible person segments, secondary constitution, and super-secondary constructions around the whole library. The computations concerned are NP-hard within the normal case (3D-3D). speedy certain recursions for the limited series singleton-only (1D-3D) case are given. Conclusions comprise: (a) the main possible joint center constitution and alignment isn't really unavoidably the main possible alignment of the main possible middle constitution, yet particularly maximizes the made of center and alignment chances; (b) use of a sequence-independent linear or affine hole penalty may end up within the highest-probability threading now not having the bottom rating; (c) deciding on the main possible center constitution from the library (core constitution choice or fold reputation merely) comprises evaluating possibilities summed over all attainable alignments of the series to the center, and never evaluating person optimum (or near-optimal) sequence-structure alignments; and (d) assuming uninformative priors, middle constitution choice is comparable to evaluating the ratio of 2 worldwide potential.
Read Online or Download A Bayes-optimal sequence-structure theory that unifies protein sequence-structure recognition and alignment PDF
Similar biotechnology books
Computational modeling is rising as a strong new method of examine and control organic platforms. a number of tools were built to version, visualize, and rationally regulate structures at quite a few size scales, ranging from molecular modeling and layout at atomic answer to mobile pathways modeling and research.
Up to now decade, there was great growth in maize biotechnology. This quantity offers an summary of our present wisdom of maize molecular genetics, the way it is getting used to enhance the crop, and destiny percentages for crop enhancement. a number of chapters care for genetically engineered qualities which are at present, or quickly can be, in advertisement creation.
There were quick advances within the box of plant biotechnology in recent times, expanding the opportunity of scientific program. overlaying the most recent advances within the use of crops to supply medications and vaccines, this quantity examines issues together with plant tissue tradition, secondary metabolite creation, metabolomics and metabolic engineering, bioinformatics, molecular farming and destiny biotechnological instructions, with members from key researchers within the box.
Right here, the world's most sensible specialists impart their wisdom and adventure, many in print for the 1st time. via contemplating constructing state markets, this booklet is the 1st actually worldwide advisor to expertise move, aiding businesses all over the international to prevent high priced errors in product improvement and to recuperate investments speedy.
- Biotechnolgy Annual Review
- The Biotechnology Directory 1997
- New Developments in Biotechnology
- Interdisciplinary Reviews - Nanomedicine and Nanobiotechnology
- Comprehensive Biotechnology-I: Cell Biology and Genetics
- Nanoscience and Nanoengineering: Advances and Applications
Additional resources for A Bayes-optimal sequence-structure theory that unifies protein sequence-structure recognition and alignment
Sander (1996). Mapping the protein universe. Science 273, 595-602. Hunter, L. and D. J. States (1992). Bayesian classification of protein structure. IEEE A Bayes-optimal Sequence-structure Theory 1069 Expert 7, 67-75. Jernigan, R. L. and I. Bahar (1996). Structure-derived potentials and protein simulations. Current Opinion in Structural Biol. 6, 195-209. Jones, D. , W. R. Taylor and J. M. Thornton (1992). A new approach to protein fold recognition. Nature (London) 358, 8689. Jones, D. T. and J.
Karplus and B. M. Pettitt (1990). Proteins: A Theoretical Perspective of Dynamics, Structure, and Thermodynamics, New York: John Wiley and Sons. Bryant, S. H. and S. F. Altschul (1995). Statistics of sequence-structure threading. Current Opinion in Structural Biol. 5, 236-244. Bryant, S. H. and C. E. Lawrence (1993). An empirical energy function for threading protein sequence through the folding motif. Proteins; Structure, Function, and Genetics 16, 92-112. Crippen, G. M. (1996). Failures of inverse folding and threading with gapped alignment.
Rosenfeld, S. Vajda and C. DeLisi (1993). Determining protein loop conformation using scaling-relaxation techniques. Protein Sci. 2, 1242- 1248.
A Bayes-optimal sequence-structure theory that unifies protein sequence-structure recognition and alignment by Lathrop R. H., Rogers Jr R. G., Smith T. F.