Predicting the solvent accessibility of transmembrane residues from protein sequence.
about
Predicting helix-helix interactions from residue contacts in membrane proteinsComputational modeling of membrane proteinsComputing structure-based lipid accessibility of membrane proteins with mp_lipid_acc in RosettaMP.A sequence-based computational model for the prediction of the solvent accessible surface area for α-helix and β-barrel transmembrane residues.Prediction of the exposure status of transmembrane beta barrel residues from protein sequence.Transmembrane protein alignment and fold recognition based on predicted topologyPrediction of the burial status of transmembrane residues of helical membrane proteins.Optimal mutation sites for PRE data collection and membrane protein structure prediction.A comparative study of the second-order hydrophobic moments for globular proteins: the consensus scale of hydrophobicity and the CHARMM partial atomic chargesSequence based residue depth prediction using evolutionary information and predicted secondary structureRecognition of interaction interface residues in low-resolution structures of protein assemblies solely from the positions of C(alpha) atoms.MPRAP: an accessibility predictor for a-helical transmembrane proteins that performs well inside and outside the membraneIntegrated prediction of one-dimensional structural features and their relationships with conformational flexibility in helical membrane proteins.Lipid exposure prediction enhances the inference of rotational angles of transmembrane helices.Combining secondary-structure and protein solvent-accessibility predictions in methionine substitution for anomalous dispersion.Computational studies of membrane proteins: models and predictions for biological understanding.Accurate prediction of the burial status of transmembrane residues of α-helix membrane protein by incorporating the structural and physicochemical features.Accurate Prediction of Contact Numbers for Multi-Spanning Helical Membrane Proteins.Structural determinants and functional consequences of protein affinity for membrane rafts.Predicting disulfide connectivity from protein sequence using multiple sequence feature vectors and secondary structure.Determination of Hydrophobic Lengths of Membrane Proteins with the HDGB Implicit Membrane Model.
P2860
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P2860
Predicting the solvent accessibility of transmembrane residues from protein sequence.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Predicting the solvent accessibility of transmembrane residues from protein sequence.
@ast
Predicting the solvent accessibility of transmembrane residues from protein sequence.
@en
type
label
Predicting the solvent accessibility of transmembrane residues from protein sequence.
@ast
Predicting the solvent accessibility of transmembrane residues from protein sequence.
@en
prefLabel
Predicting the solvent accessibility of transmembrane residues from protein sequence.
@ast
Predicting the solvent accessibility of transmembrane residues from protein sequence.
@en
P2093
P356
P1476
Predicting the solvent accessibility of transmembrane residues from protein sequence.
@en
P2093
Fasheng Zhang
Melissa J Davis
Zheng Yuan
P304
P356
10.1021/PR050397B
P577
2006-05-01T00:00:00Z