Suggested Reading
An unprepared physical scientist entering a conversation about biointerfaces faces multiple challenges, not the least of which is a complete new set of concepts and jargon. The resources listed on this page provide an introduction to the basics of biology relevant for biointerface research. The style and format of these books and lecture notes are well suited even for students and researchers with minimal background in life sciences.
The Physical Basis of Biochemistry
The Physical Basis of Biochemistry: The Foundations of Molecular Biophysics
by Peter R. Bergethon
Springer, 1998
ISBN 0387982620, 9780387982625
Preview on Google Books
As the title suggests, The Physical Basis of Biochemistry was written as an introductory Physics textbook for biochemists. But when read in a rearranged order, the book becomes an introduction to Biochemistry for physicists.
After an introduction to the principles of Physics and Chemistry, the book covers many important and advanced topics in Biochemistry. The chapter on each topic starts with a basic overview of the relevant biology, which is followed by a detailed description of the associated problems that can be addressed by methods from physics and chemistry. Having each of the advanced topics described using terminology and concepts from both physical and life sciences can serve as a helpful "translation" between the two sides.
For example, a chapter on Macromolecules in Solution begins by summarizing the basic chemical and biological properties of Peptides and Proteins and Nucleic Acids. Later in the chapter, the important problem of Protein Folding is described as it is seen both in biochemistry and in physical sciences, thus helping the reader to bridge the gap between the two viewpoints in terms of terminology and implicit assumptions.
Basic Concepts in Biochemistry
Basic Concepts in Biochemistry: A Student's Survival Guide
by Hiram F. Gilbert
McGraw-Hill Professional, 1999
ISBN 0071356576, 9780071356572
Preview on Google Books
This short book covers a lot of material, so it can be very useful for learning about the basic terminology and concepts from Biochemistry. To help the reader, the most critical items are highlighted in text boxes.
HYDROPHOBIC INTERACTION
Proteins fold in order to put as much of the greasy stuff out of contact with water as possible. This provides much of the "driving force" for protein folding, protein–protein interactions, and protein–ligand interactions.
The clear style is particularly helpful for explaining concepts that involve many categories.
SECONDARY STRUCTURE
Secondary structure is not just hydrogen bonds.
α Helix: Right-handed helix with 3.6 amino acid residues per turn. Hydrogen bonds are formed parallel to the helix axis.
β Sheet: A parallel or antiparallel arrangement of the polypeptide chain. Hydrogen bonds are formed between the two (or more) polypeptide strands.
β Turn: A structure in which the polypeptide backbone folds back on itself. Turns are useful for connecting helices and sheets.