Urea gradient polyacrylamide gel electrophoresis and folding analysis experiments
Goldenberg and Creighfn (1984) introduced the use of polyacrylamide gels containing a concentration gradient of urea to analyze the folded state of proteins. A
3,200+ step-by-step lab protocols and SOPs for cell culture, staining, PCR, protein work and microbiology, with reagents, conditions and evaluation criteria.
Goldenberg and Creighfn (1984) introduced the use of polyacrylamide gels containing a concentration gradient of urea to analyze the folded state of proteins. A
This experiment describes the trypsin digestion process of calmodulin. This experiment was derived from Protein Purification and Identification Laboratory Guide
This experiment describes the fragmentation of E. coli cells and the preparation of inclusion bodies. This experiment is from the Laboratory Guide for Protein P
In this experiment, nuclear extracts were prepared from HeLa cells essentially as described by Dignam et al. (1983). This basic method is probably the most comm
This experiment describes the preparation process of DNA affinity medium. This experiment is from the Laboratory Guide for Protein Purification and Characteriza
This experiment introduces the related operation of affinity chromatography. This experiment is from the Laboratory Guide for Protein Purification and Identific
There is a great need for a rapid and accurate method for quantitatively determining the protein concentration in a sample so that one can follow the recovery o
In this unit, a simpler method was used to determine its stimulatory effect on core RNA polymerase transcription from a non-specific template poly(dAT) start. T
In this experiment, we used the same complementary oligonucleotide used for DNA affinity chromatography (see the end of the Introduction to Experiment 3 for the