[HTML][HTML] The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy

B Bechinger - Biochimica et Biophysica Acta (BBA)-Biomembranes, 1999 - Elsevier
Linear peptide antibiotics have been isolated from amphibians, insects and humans and
used as templates to design cheaper and more potent analogues for medical applications …

Chemical shift tensor–The heart of NMR: Insights into biological aspects of proteins

H Saitô, I Ando, A Ramamoorthy - Progress in nuclear magnetic resonance …, 2010 - Elsevier
The chemical shift of a nucleus, i, in a molecule arises from the nuclear shielding effect of an
applied magnetic field, caused by an induced magnetic field resulting from circulation of …

Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR

JJ Balbach, Y Ishii, ON Antzutkin, RD Leapman… - Biochemistry, 2000 - ACS Publications
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH2, called Aβ16-22
and representing residues 16− 22 of the full-length β-amyloid peptide associated with …

Backbone Dynamics ofEscherichia coliRibonuclease HI: Correlations with Structure and Function in an Active Enzyme

AM Mandel, M Akke, AG Palmer III - Journal of molecular biology, 1995 - Elsevier
Ribonuclease H is an endonuclease that hydrolyzes the RNA moiety of RNA–DNA duplex
molecules. Escherichia coliribonuclease H is involved in DNA replication, and retroviral …

Structure and orientation of the antibiotic peptide magainin in membranes by solid‐state nuclear magnetic resonance spectroscopy

B Bechinger, M Zasloff, SJ Opella - Protein Science, 1993 - Wiley Online Library
Magainin 2 is a 23‐residue peptide that forms an amphipathic α‐helix in membrane
environments. It functions as an antibiotic and is known to disrupt the electrochemical …

[PDF][PDF] Imaging membrane protein helical wheels

J Wang, J Denny, C Tian, S Kim, Y Mo, F Kovacs… - Journal of Magnetic …, 2000 - mit.edu
Macromolecular structure determination by NMR spectroscopy has been absolutely
dependent on resonance assignments. Indeed, inaccurate assignments have frequently led …

Direct measurement of angles between bond vectors in high-resolution NMR

B Reif, M Hennig, C Griesinger - Science, 1997 - science.org
Angles between two interatomic vectors are measured for structure elucidation in solution
nuclear magnetic resonance (NMR). The angles can be determined directly by using the …

A robust technique for two-dimensional separation of undistorted chemical-shift anisotropy powder patterns in magic-angle-spinning NMR

SF Liu, JD Mao, K Schmidt-Rohr - Journal of Magnetic Resonance, 2002 - Elsevier
A robust magic-angle-spinning experiment for separating undistorted, quasi-static chemical-
shift powder patterns is presented. It is derived from the technique of R. Tycko, G. Dabbagh …

Towards membrane protein design: pH-sensitive topology of histidine-containing polypeptides

B Bechinger - Journal of molecular biology, 1996 - Elsevier
Hydrophobic and amphipathic α-helices act as independent functional units in immunogenic
or fusogenic polypeptides and constitute important structural building blocks in larger …

NMR studies of Brownian tumbling and internal motions in proteins

DM Korzhnev, M Billeter, AS Arseniev… - Progress in Nuclear …, 2001 - Elsevier
2.1. 2. Green function for rigid body diffusion.................................... 225 2.1. 3. NMR correlation
functions............................................. 226 2.2. Calculations of the diffusion …