Infrared spectroscopy of proteins.

We have used the pH-induced self-assembly of a peptide-amphiphile to make a nanostructured fibrous scaffold reminiscent of extracellular matrix. The design of this peptide-amphiphile allows the nanofibers to be reversibly cross-linked to enhance or decrease their structural integrity. After cross-linking, the fibers are able to direct mineralization of hydroxyapatite to form a composite material in which the crystallographic c axes of hydroxyapatite are aligned with the long axes of the fibers. This alignment is the same as that observed between collagen fibrils and hydroxyapatite crystals in bone.

http://science.sciencemag.org/content/sci/294/5547/1684.full.pdf

Self-assembly and mineralization of peptide-amphiphile nanofibers

Fourier transform infrartd (FTIR) spectroscopy is an established tool for the structural character- ization of proteins. However, many potential pitfalls exist for the unwary investigator. In this review we critically assess the application of FIlR spectroscopy to the determination of protein structure by (1) outlining the principles underlying protein secondary structure determination by FZZR spectroscopy. (2) highhghting the situations in which FZZR spectroscopy should be considered the technique of choice, (3) discussing the manner in which experiments should be conducted to derive as much physiologically relevant information as possible, and (4) outlining current methods for the determination of secondary structure from infrared spectm of proteins,

The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure

This review deals with current concepts of vibrational spectroscopy for the investigation of protein structure and function. While the focus is on infrared (IR) spectroscopy, some of the general aspects also apply to Raman spectroscopy. Special emphasis is on the amide I vibration of the polypeptide backbone that is used for secondary-structure analysis. Theoretical as well as experimental aspects are covered including transition dipole coupling. Further topics are discussed, namely the absorption of amino-acid side-chains, 1H/2H exchange to study the conformational flexibility and reaction-induced difference spectroscopy for the investigation of reaction mechanisms with a focus on interpretation tools.

https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0033583502003815

What vibrations tell us about proteins

Membranes are the most common cellular structures in both plants and animals. They are now recognized as being involved in almost all aspects of cellular activity ranging from motility and food entrapment in simple unicellular organisms, to energy transduction, immunorecognition, nerve conduction and biosynthesis in plants and higher organisms. This functional diversity is reflected in the wide variety of lipids and particularly of proteins that compose different membranes. An understanding of the physical principles that govern the molecular organization of membranes is essential for an understanding of their physiological roles since structure and function are much more interdependent in membranes than in, say, simple chemical reactions in solution. We must recognize, however, that the word ‘understanding’ means different things in different disciplines, and nowhere is this more apparent than in this multidisciplinary area where biology, chemistry and physics meet.

/pdf/physical-principles-of-membrane-organization-2enzb9mlqb.pdf

Physical principles of membrane organization.

Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment.

Theoretical Analyses of the Amide I Infrared Bands of Globular Proteins (H. Torii & M. Tasumi). Fourier Transform Infrared Spectroscopy of Enzyme Systems (J. Alben). Light--Induced Fourier Transform Infrared Difference Spectroscopy of the Primary Electron Donor in Photosynthetic Reaction Centers (E. Nabedryk). Equipment: Slow and Fast Infrared Kinetic Studies (F. Siebert). Ultrafast Infrared Spectroscopy of Biomolecules (B. Cohen & R. Hochstrasser). Infrared Spectroscopy of Nucleic Acids (J. Liquier & E. Taillandier). Fourier Transform Infrared Spectroscopy in the Study of Hydrated Lipids and Lipid Bilayer Membranes (R. Lewis & R. McElhaney). Fourier Transform Infrared Spectroscopic Studies of Cell Surface Polysaccharides (K. Brandenburg & U. Seydel). Fourier Transform Infrared Spectroscopy of Biomembrane Systems (P. Haris & D. Chapman). What Can Infrared Spectroscopy Tell Us About the Structure and Composition of Intact Bacterial Cells? (D. Naumann, et al.). Biomedical Infrared Spectroscopy (M. Jackson & H. Mantsch). New Trends in Isotope--Edited Infrared Spectroscopy (H. Fabian, et al.). Index.

Infrared spectroscopy of biomolecules

Deuterium Fourier transform nuclear magnetic resonance (NMR) spectra at 34 MHz (corresponding to a magnetic field strength of 5.2 T) have been obtained of a variety of protein-lipid systems containing specifically deu- terated phospholipids. The following systems were investigated as a function of temperature: sarcoplasmic reticulum ATPase (ATP phosphohydrolase, EC 3.6.1.3) complexed with 1- myristoyl-2-( 14,14,14-trideuteriomyristoyl)-sn-glycero-3- phosphocholine (DMPC-d3) or 1,2-bis( 16,16,16-trideuterio- palmitoyl)-sn-glycero-3-phosphocholine (DPPC-d,); human brain lipophilin complexed with DPPC-d6 or 1,2-bis(6,6-di-

/pdf/protein-lipid-interactions-a-nuclear-magnetic-resonance-5ag04glmns.pdf

Protein-lipid interactions. A nuclear magnetic resonance study of sarcoplasmic reticulum (calcium(2+), magnesium(2+) ion)-activated ATPase, lipophilin, and proteolipid apoprotein-lecithin systems and a comparison with the effects of cholesterol

Dennis Chapman

Papers

Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment.

Infrared spectroscopy of biomolecules

Protein-lipid interactions. A nuclear magnetic resonance study of sarcoplasmic reticulum (calcium(2+), magnesium(2+) ion)-activated ATPase, lipophilin, and proteolipid apoprotein-lecithin systems and a comparison with the effects of cholesterol