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Current Protocols in Protein Science is a peer-reviewed journal published by Wiley, covering Advanced Proteomics Techniques and Applications, Mass Spectrometry Techniques and Applications, Protein purification and stability.
| Publisher | Wiley |
|---|---|
| Reference style | Author–year (Chicago) Author–year — (Smith, 2023) in the text Smith, Ada, Ben Jones, and Cara Lee. 2023. "A Representative Article Title." Current Protocols in Protein Science 12 (3): 45–58.
Formats any DOI in Current Protocols in Protein Science style. No sign-up. |
| Publishes research in | Advanced Proteomics Techniques and Applications Mass Spectrometry Techniques and Applications Protein purification and stability Protein Structure and Dynamics Glycosylation and Glycoproteins Research |
| ISSN | 1934-3655 |
| h-index | 64 |
| i10-index | 333 |
| Total citations | 21,480 |
| Article processing charge | $5,050 |
| Top institutions publishing here | National Institutes of Health |
| Journal website | currentprotocols.onlinelibrary.wiley.com |
| You get | A submission-ready PDF and the editable LaTeX source — ready to submit. |
Citations each year’s papers have accumulated so far — the most recent years are still building up.
Functional characterization of a protein sequence is a common goal in biology, and is usually facilitated by having an accurate three-dimensional (3-D) structure of the studied protein. In the absence of an experimentally determined structure, comparative or homology modeling can sometimes provide a useful 3-D model for a protein that is related to at least…
Abstract Comparative protein structure modeling predicts the three‐dimensional structure of a given protein sequence (target) based primarily on its alignment to one or more proteins of known structure (templates). The prediction process consists of fold assignment, target‐template alignment, model building, and model evaluation. This unit describes how to calculate comparative models using the program MODELLER…
Purification of recombinant proteins for biochemical assays and structural studies is time-consuming and presents inherent difficulties that depend on the optimization of protein stability. The use of dyes to monitor thermal denaturation of proteins with sensitive fluorescence detection enables rapid and inexpensive determination of protein stability using real-time PCR instruments. By screening a wide range…
BioID is a unique method to screen for physiologically relevant protein interactions that occur in living cells. This technique harnesses a promiscuous biotin ligase to biotinylate proteins based on proximity. The ligase is fused to a protein of interest and expressed in cells, where it biotinylates proximal endogenous proteins. Because it is a rare protein…
Abstract BioID is a unique method to screen for physiologically relevant protein interactions that occur in living cells. This technique harnesses a promiscuous biotin ligase to biotinylate proteins based on proximity. The ligase is fused to a protein of interest and expressed in cells, where it biotinylates proximal endogenous proteins. Because it is a rare…
