hp lattice
Recently Published Documents


TOTAL DOCUMENTS

25
(FIVE YEARS 2)

H-INDEX

7
(FIVE YEARS 0)

2021 ◽  
Vol 8 (3) ◽  
pp. 291-306
Author(s):  
Salomón J. Alas-Guardado ◽  
◽  
Pedro Pablo González-Pérez ◽  
Hiram Isaac Beltrán ◽  
◽  
...  

<abstract> <p>Many of the simplistic hydrophobic-polar lattice models, such as Dill's model (called <bold>Model 1</bold> herein), are aimed to fold structures through hydrophobic-hydrophobic interactions mimicking the well-known hydrophobic collapse present in protein structures. In this work, we studied 11 designed hydrophobic-polar sequences, S<sub>1</sub>-S<sub>8</sub> folded in 2D-square lattice, and S<sub>9</sub>-S<sub>11</sub> folded in 3D-cubic lattice. And to better fold these structures we have developed <bold>Model 2</bold> as an approximation to convex function aimed to weight hydrophobic-hydrophobic but also polar-polar contacts as an augmented version of <bold>Model 1</bold>. In this partitioned approach hydrophobic-hydrophobic ponderation was tuned as <italic>α</italic>-1 and polar-polar ponderation as <italic>α</italic>. This model is centered in preserving required hydrophobic substructure, and at the same time including polar-polar interactions, otherwise absent, to reach a better folding score now also acquiring the polar-polar substructure. In all tested cases the folding trials were better achieved with <bold>Model 2</bold>, using <italic>α</italic> values of 0.05, 0.1, 0.2 and 0.3 depending of sequence size, even finding optimal scores not reached with <bold>Model 1</bold>. An important result is that the better folding score, required the lower <italic>α</italic> weighting. And when <italic>α</italic> values above 0.3 are employed, no matter the nature of the hydrophobic-polar sequence, banning of hydrophobic-hydrophobic contacts started, thus yielding misfolding of sequences. Therefore, the value of <italic>α</italic> to correctly fold structures is the result of a careful weighting among hydrophobic-hydrophobic and polar-polar contacts.</p> </abstract>


2018 ◽  
Vol 44 (12) ◽  
pp. 1025-1030
Author(s):  
Matthew S. Wilson ◽  
Guangjie Shi ◽  
Thomas Wüst ◽  
Ying Wai Li ◽  
David P. Landau

2015 ◽  
Vol 640 ◽  
pp. 012015 ◽  
Author(s):  
Busara Pattanasiri ◽  
Ying Wai Li ◽  
Thomas Wust ◽  
David P Landau

2014 ◽  
Vol 11 (95) ◽  
pp. 20140249 ◽  
Author(s):  
Sam F. Greenbury ◽  
Iain G. Johnston ◽  
Ard A. Louis ◽  
Sebastian E. Ahnert

The mapping between biological genotypes and phenotypes is central to the study of biological evolution. Here, we introduce a rich, intuitive and biologically realistic genotype–phenotype (GP) map that serves as a model of self-assembling biological structures, such as protein complexes, and remains computationally and analytically tractable. Our GP map arises naturally from the self-assembly of polyomino structures on a two-dimensional lattice and exhibits a number of properties: redundancy (genotypes vastly outnumber phenotypes), phenotype bias (genotypic redundancy varies greatly between phenotypes), genotype component disconnectivity (phenotypes consist of disconnected mutational networks) and shape space covering (most phenotypes can be reached in a small number of mutations). We also show that the mutational robustness of phenotypes scales very roughly logarithmically with phenotype redundancy and is positively correlated with phenotypic evolvability. Although our GP map describes the assembly of disconnected objects, it shares many properties with other popular GP maps for connected units, such as models for RNA secondary structure or the hydrophobic-polar (HP) lattice model for protein tertiary structure. The remarkable fact that these important properties similarly emerge from such different models suggests the possibility that universal features underlie a much wider class of biologically realistic GP maps.


Sign in / Sign up

Export Citation Format

Share Document