Basics: The biochemistry of protein interactions and structure
Proteins are complex and dynamic three dimensional molecules that work in groups and can change each other. Proteins interact with themselves and other proteins via different forms of intra (within the same protein) and inter (between proteins) molecular forces that...
Basics: Removing lipids and detergents from peptide samples
When trying to remove one class of molecules from another then you need to look for chemical characteristics that can be used to differentiate between them. In the case of the removal of lipids and detergents from protein samples then the best opportunity for success...
Basics: Lipids and detergents and their effect on LC-MS
We have had increasing evidence that non-peptide molecules are coming through our sample prep techniques and affecting the LC-MS systems. We are pretty sure about the effect of triton and other detergents such as CHAPS but similar effects from samples that do not...
Facility: Is accuracy important?
This post follows on from a conversation with Christoph Borchers of the University of Vancouver in which he states “Accuracy is not important, precision is everything”. This is a highly provocative statement, especially in the analytical world but is he right?To begin...
Basics: Protein solubilisation
To solubilise proteins you need to break proteins apart (see guide to protein-protein interactions for details on the forces that keep proteins together) and keep them apart. Breaking proteins apartBreaking proteins apart has two main components, physical disruption...
Basics: How mass spectrometry is used to identify and characterise proteins
There are a number of ways in which mass spectrometry can be used to identify and characterise proteins but the method used in Bio-MS is the most common method using fragmentation data from peptides. As well as scanning the masses and intensities of the ions present a...
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