A physical reference state unifies the structure-derived potential of mean force for protein folding and binding

2004 ◽  
Vol 56 (1) ◽  
pp. 93-101 ◽  
Author(s):  
Song Liu ◽  
Chi Zhang ◽  
Hongyi Zhou ◽  
Yaoqi Zhou
Keyword(s):  
Protein Folding ◽  
Potential Of Mean Force ◽  
Reference State

scholarly journals Orientation-dependent potential of mean force for protein folding

2005 ◽  
Vol 123 (1) ◽  
pp. 014901 ◽  
Author(s):  
Arnab Mukherjee ◽  
Prabhakar Bhimalapuram ◽  
Biman Bagchi
Keyword(s):  
Protein Folding ◽  
Potential Of Mean Force ◽  
Dependent Potential

Spatial localization of unknown proteins in the endoplasmic reticulum predicts functions

2007 ◽  
Vol 30 (4) ◽  
pp. 84
Author(s):  
Michael D. Jain ◽  
Hisao Nagaya ◽  
Annalyn Gilchrist ◽  
Miroslaw Cygler ◽  
John J.M. Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Synthesis ◽  
Protein Function ◽  
Protein Translocation ◽  
Spatial Localization ◽  
Predict Protein Function ◽  
Insight Into ◽  
Soluble Fractions ◽  
Er Membrane

Protein synthesis, folding and degradation functions are spatially segregated in the endoplasmic reticulum (ER) with respect to the membrane and the ribosome (rough and smooth ER). Interrogation of a proteomics resource characterizing rough and smooth ER membranes subfractionated into cytosolic, membrane, and soluble fractions gives a spatial map of known proteins involved in ER function. The spatial localization of 224 identified unknown proteins in the ER is predicted to give insight into their function. Here we provide evidence that the proteomics resource accurately predicts the function of new proteins involved in protein synthesis (nudilin), protein translocation across the ER membrane (nicalin), co-translational protein folding (stexin), and distal protein folding in the lumen of the ER (erlin-1, TMX2). Proteomics provides the spatial localization of proteins and can be used to accurately predict protein function.

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