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 …

Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37

KA Henzler Wildman, DK Lee, A Ramamoorthy - Biochemistry, 2003 - ACS Publications
LL-37 is an amphipathic, α-helical, antimicrobial peptide. 15N chemical shift and 15N
dipolar− shift spectroscopy of site-specifically labeled LL-37 in oriented lipid bilayers …

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 …

Probing hydrogen bonding in solids using solid state NMR spectroscopy

AE Aliev, KDM Harris - Supramolecular Assembly via Hydrogen Bonds I, 2004 - Springer
Solid state nuclear magnetic resonance (NMR) spectroscopy is a powerful and versatile
technique for probing structural and dynamic properties of solid materials, and can provide …

Chemical shifts in proteins come of age

L Szilágyi - Progress in Nuclear Magnetic Resonance …, 1995 - Elsevier
2.1 'H shifts 2.1. 1 Her, H/I and HN secondary structure shifts 2.1. 2 'H shift regularities in
helices 2.1. 2.1 Helix dipole effects 2.1. 2.2 Periodicity of HG (and HN shifts 2.2 Secondary …

Solid-State 15N NMR Chemical Shift Anisotropy of Histidines:  Experimental and Theoretical Studies of Hydrogen Bonding

Y Wei, AC de Dios, AE McDermott - Journal of the American …, 1999 - ACS Publications
The principal values of the 15N chemical shift tensors of crystalline histidine and histidine-
containing peptides have been measured to document for the first time the systematic trends …

[HTML][HTML] Conformation of alamethicin in oriented phospholipid bilayers determined by 15N solid-state nuclear magnetic resonance

M Bak, RP Bywater, M Hohwy, JK Thomsen… - Biophysical …, 2001 - cell.com
The conformation of the 20-residue antibiotic ionophore alamethicin in macroscopically
oriented phospholipid bilayers has been studied using 15 N solid-state nuclear magnetic …

Complexes obtained by electrophilic attack on a dinitrogen-derived terminal molybdenum nitride: electronic structure analysis by solid state CP/MAS 15N NMR in …

EL Sceats, JS Figueroa, CC Cummins, NM Loening… - Polyhedron, 2004 - Elsevier
15N Solid state CP/MAS NMR spectroscopy has been used to study a dinitrogen-derived
terminal nitride of molybdenum, 15NMo (N [tBu] Ar) 3 (Ar= 3, 5-(CH3) 2C6H3). A number of …

NMR study of silk I structure of Bombyx mori silk fibroin with 15N‐ and 13C‐NMR chemical shift contour plots

T Asakura, M Demura, T Date… - Biopolymers …, 1997 - Wiley Online Library
The metastable state silk I structures of Bombyx mori silk fibroin in the solid state were
studied on the basis of 15N‐and 13C‐nmr chemical shifts of Ala, Ser, and Gly residues. The …

Analyzing atomic scale structural details and nuclear spin dynamics of four macrolide antibiotics: erythromycin, clarithromycin, azithromycin, and roxithromycin

BL Pradhan, L Lodhi, KK Dey, M Ghosh - RSC advances, 2024 - pubs.rsc.org
The current investigation centers on elucidating the intricate molecular architecture and
dynamic behavior of four macrolide antibiotics, specifically erythromycin, clarithromycin …