Nano-chemical infrared imaging of membrane proteins in lipid bilayers.

نویسندگان

  • Samuel Berweger
  • Duc M Nguyen
  • Eric A Muller
  • Hans A Bechtel
  • Thomas T Perkins
  • Markus B Raschke
چکیده

The spectroscopic characterization of biomolecular structures requires nanometer spatial resolution and chemical specificity. We perform full spatio-spectral imaging of dried purple membrane patches purified from Halobacterium salinarum with infrared vibrational scattering-type scanning near-field optical microscopy (s-SNOM). Using near-field spectral phase contrast based on the Amide I resonance of the protein backbone, we identify the protein distribution with 20 nm spatial resolution and few-protein sensitivity. This demonstrates the general applicability of s-SNOM vibrational nanospectroscopy, with potential extension to a wide range of biomolecular systems.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

اثرات میدان الکترومغناطیسی تلفن همراه بر عملکرد تک نانوکانال پروتیینی OmpF: یک رویکرد تجربی

Background: Widespread of telecommunication systems in recent years, have raised the concerns on the possible danger of cell phone radiations on human body. Thus, the study of the electromagnetic fields on proteins, particularly the membrane nano channel forming proteins is of great importance. These proteins are responsible for keeping certain physic-chemical condition within cells and managin...

متن کامل

Characterization of biophysical properties of single chloride channel in rat brain mitochondrial inner membrane by channel incorporation into bilayer lipid membrane

Introduction: Recent studies have shown the presence of Cl- channels in heart and liver mitochondrial membranes. In this work, we have characterized the functional profile of a Cl- channel from rat brain mitochondria. Methods: After removing and homogenizing the rat brain, the supernatant was separately centrifuged in MSEdigitonin, H2O and Na2CO3 and mitochondrial inner membrane vesicles wer...

متن کامل

Molecular Insight into the Mutual Interactions of Two Transmembrane Domains of Human Glycine Receptor (TM23-GlyR), with the Lipid Bilayers

Appearing as a computational microscope, MD simulation can ‘zoom in’ to atomic resolution to assess detailed interactions of a membrane protein with its surrounding lipids, which play important roles in the stability and function of such proteins. This study has employed the molecular dynamics (MD) simulations, to determine the effect of added DMPC or DMTAP molecules on the structure of D...

متن کامل

Oriented attachment and membrane reconstitution of His-tagged cytochrome c oxidase to a gold electrode: in situ monitoring by surface-enhanced infrared absorption spectroscopy.

A novel concept is introduced for the oriented incorporation of membrane proteins into solid supported lipid bilayers. Recombinant cytochrome c oxidase solubilized in detergent was immobilized on a chemically modified gold surface via the affinity of its histidine-tag to a nickel-chelating nitrilo-triacetic acid (NTA) surface. The oriented protein monolayer was reconstituted into the lipid envi...

متن کامل

Solid-state NMR studies of the structure, dynamics, and assembly of beta-sheet membrane peptides and alpha-helical membrane proteins with antibiotic activities.

beta-Sheet antimicrobial peptides and alpha-helical channel-forming colicins are bactericidal molecules that target the lipid membranes of sensitive cells. Understanding the mechanisms of action of these proteins requires knowledge of their three-dimensional structure in the lipid bilayer. Solid-state NMR has been used to determine the conformation, orientation, depth of insertion, oligomerizat...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Journal of the American Chemical Society

دوره 135 49  شماره 

صفحات  -

تاریخ انتشار 2013