scholarly article | Q13442814 |
P356 | DOI | 10.1016/0005-2736(79)90096-8 |
P953 | full work available at URL | https://api.elsevier.com/content/article/PII:0005273679900968?httpAccept=text/xml |
https://api.elsevier.com/content/article/PII:0005273679900968?httpAccept=text/plain | ||
P698 | PubMed publication ID | 549631 |
P2093 | author name string | L. R. Brown | |
P2860 | cites work | Biochimica et Biophysica Acta | Q864239 |
Interaction of phospholipase A2 with micellar interfaces. Role of the N-terminal region | Q30104786 | ||
Specificity of interproton nuclear Overhauser effects in gramicidin-S dissolved in deuterated ethylene glycol | Q34656425 | ||
1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI) | Q39163947 | ||
Allergens of honey bee venom | Q39374694 | ||
NMR observation of gramicidin A' in phosphatidylcholine vesicles | Q39460734 | ||
Hydrogen exchange | Q39919670 | ||
NMR and ESR studies of the interactions of cytochrome c with mixed cardiolipin-phosphatidylcholine vesicles | Q40082908 | ||
Structure and thermodynamic properties of the complexes between phospholipase A2 and lipid micelles | Q41439390 | ||
Comparison of membrane organization in mitochondria from yeast and rat liver by nuclear magnetic resonance spectroscopy | Q43802156 | ||
Proton magnetic resonance spectroscopy of promitochondrial membranes from yeast grown under different regimes of lipid supplementation | Q44772125 | ||
13C nuclear magnetic resonance study of molecular motions and conformational transitions in muscle calcium binding parvalbumins | Q45236449 | ||
Interaction of glucagon with dimyristoyl glycerophosphocholine. | Q53731017 | ||
Action of phospholipases on the cytoplasmic membrane of Escherichia coli. Stimulation by melittin | Q67474741 | ||
P433 | issue | 1 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | biochemistry | Q7094 |
biophysics | Q7100 | ||
cell biology | Q7141 | ||
apitoxin | Q423888 | ||
melittin | Q424512 | ||
micelles | Q421110 | ||
membrane protein | Q423042 | ||
P304 | page(s) | 135-148 | |
P577 | publication date | 1979-10-01 | |
1979-10-19 | |||
P1433 | published in | Biochimica et Biophysica Acta | Q864239 |
P1476 | title | Use of fully deuterated micelles for conformational studies of membrane proteins by high resolution 1H nuclear magnetic resonance | |
P478 | volume | 557 |
Q71845637 | An NMR Study of the Interaction of Cardiotoxin gamma from Naja nigricollis with Perdeuterated Dodecylphosphocholine Micelles |
Q48944692 | Binding of myelin basic protein to phospholipid micelles |
Q42244998 | Combined use of proton-proton overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon |
Q34256383 | Comparative effects of melittin and its hydrophobic and hydrophilic fragments on bilayer organization by Raman spectroscopy |
Q27729151 | Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance |
Q72864525 | Conformational studies of lipid-bound polypeptides by elucidation of proton-proton cross-relaxation networks |
Q34088688 | Customizing model membranes and samples for NMR spectroscopic studies of complex membrane proteins |
Q30925783 | Dynamic properties of salmon calcitonin bound to sodium dodecyl sulfate micelles: a restrained molecular dynamics study from NMR data |
Q46596690 | Estimation of deuteration levels in whole cells and cellular proteins by 1H n.m.r. spectroscopy and neutron scattering |
Q28366140 | High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface |
Q36664481 | High-resolution 1H-NMR studies of monomeric melittin in aqueous solution |
Q36664485 | High-resolution 1H-NMR studies of self-aggregation of melittin in aqueous solution |
Q67658605 | Interactions of myelin basic protein with mixed dodecylphosphocholine/palmitoyllysophosphatidic acid micelles |
Q72908108 | Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine EPR and NMR studies |
Q70968069 | Melittin bound to dodecylphosphocholine micelles 1H-NMR assignments and global conformational features |
Q30332957 | Membrane protein dynamics versus environment: simulations of OmpA in a micelle and in a bilayer. |
Q30418952 | Methods to study membrane protein structure in solution |
Q36281647 | NMR studies of the low-density lipoprotein receptor-binding peptide of apolipoprotein E bound to dodecylphosphocholine micelles |
Q42223425 | Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles |
Q34251677 | Nuclear magnetic resonance of the filamentous bacteriophage fd |
Q32119117 | Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study |
Q42273941 | Physicochemical characterization of glucagon-containing lipid micelles |
Q72189205 | Pulmonary surfactant-associated polypeptide SP-C in lipid micelles: CD studies of intact SP-C and NMR secondary structure determination of depalmitoyl-SP-C(1-17) |
Q36244625 | Role of membrane lipids in peptide hormone function: binding of enkephalins to micelles |
Q42160638 | Secondary structure and biophysical activity of synthetic analogues of the pulmonary surfactant polypeptide SP-C |
Q42263758 | Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles. |
Q27640297 | Solution structure of the tachykinin peptide eledoisin |
Q30431300 | Structure and dynamics in proteins of pharmacological interest |
Q27621702 | The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles |
Q41867744 | The conformation of substance P in lipid environments. |
Q74567671 | The use of sodium dodecyl sulfate to model the apolipoprotein environment. Evidence for peptide-SDS complexes using pulsed-field-gradient NMR spectroscopy |
Q24537743 | Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles |