Two-intermediate model to characterize the structure of fast-folding proteins
From MaRDI portal
Recommendations
Cites work
- A high-accuracy protein structural class prediction algorithm using predicted secondary structural information
- Hydrophobic collapse in (in silico) protein folding
- Knowledge-based computational mutagenesis for predicting the disease potential of human non-synonymous single nucleotide polymorphisms
- Predicting ion channels and their types by the dipeptide mode of pseudo amino acid composition
- Prediction of protein submitochondria locations based on data fusion of various features of sequences
- Protein folding disorders: toward a basic biological paradigm
- Some remarks on protein attribute prediction and pseudo amino acid composition
- Two-intermediate model to characterize the structure of fast-folding proteins
- Using the augmented Chou's pseudo amino acid composition for predicting protein submitochondria locations based on auto covariance approach
Cited in
(8)- Equilibrium protein folding-unfolding process involving multiple intermediates
- iCDI-PseFpt: identify the channel-drug interaction in cellular networking with PseAAC and molecular fingerprints
- Hydrophobic collapse in (in silico) protein folding
- A two-fold structural classification method for determining the accurate ensemble of protein structures
- Predicting Experimental Quantities in Protein Folding Kinetics Using Stochastic Roadmap Simulation
- Analytical model for protein folding
- Two-intermediate model to characterize the structure of fast-folding proteins
- The fuzzy oil drop model, based on hydrophobicity density distribution, generalizes the influence of water environment on protein structure and function
This page was built for publication: Two-intermediate model to characterize the structure of fast-folding proteins
Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q1783656)