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Person

Riddhiman Sarkar

Chemiker

Name	Riddhiman Sarkar
Zeit	2007- (Wirkungsdaten)
Ort	Deutschland
Geschlecht	männlich
Akademischer Grad bzw. Titel	Dr.
Beruf	Chemiker (charakteristischer Beruf)
Beziehung	HelmholtzZentrum München
Datensatztyp	Person
GND-Nummer	1275936741
Datensatz-ID	1275936741
Beteiligt an alle anzeigen Multiscale Materials Engineering via Self‐Assembly of Pentapeptide Derivatives from SARS CoV E Protein SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: a MAS solid-state NMR study Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril Mapping the Binding Interface of PET Tracer Molecules and Alzheimer Disease Aβ Fibrils by Using MAS Solid‐State NMR Spectroscopy Structural Insight into IAPP‐Derived Amyloid Inhibitors and Their Mechanism of Action Structural Insight into IAPP‐Derived Amyloid Inhibitors and Their Mechanism of Action Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril MAS dependent sensitivity of different isotopomers in selectively methyl protonated protein samples in solid state NMR Determination of methyl order parameters using solid state NMR under off magic angle spinning Accurate Determination of 1 H‐ 15 N Dipolar Couplings Using Inaccurate Settings of the Magic Angle in Solid‐State NMR Spectroscopy Accurate Determination of 1 H‐ 15 N Dipolar Couplings Using Inaccurate Settings of the Magic Angle in Solid‐State NMR Spectroscopy Overcoming Volume Selectivity of Dipolar Recoupling in Biological Solid‐State NMR Spectroscopy Overcoming Volume Selectivity of Dipolar Recoupling in Biological Solid‐State NMR Spectroscopy Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins Long‐Lived States to Monitor Protein Unfolding by Proton NMR Cover Picture: Long‐Lived States to Monitor Protein Unfolding by Proton NMR (ChemPhysChem 15/2011) Berichtigung: Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization † Corrigendum: Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization † Long‐lived States in Multiple‐Spin Systems Measurement of Slow Diffusion Coefficients of Molecules with Arbitrary Scalar Couplings via Long‐Lived Spin States Extending the Scope of Singlet‐State Spectroscopy

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Katalog der Deutschen Nationalbibliothek

Riddhiman Sarkar

Multiscale Materials Engineering via Self‐Assembly of Pentapeptide Derivatives from SARS CoV E Protein

SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: a MAS solid-state NMR study

Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril

Mapping the Binding Interface of PET Tracer Molecules and Alzheimer Disease Aβ Fibrils by Using MAS Solid‐State NMR Spectroscopy

Structural Insight into IAPP‐Derived Amyloid Inhibitors and Their Mechanism of Action

Structural Insight into IAPP‐Derived Amyloid Inhibitors and Their Mechanism of Action

Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril

MAS dependent sensitivity of different isotopomers in selectively methyl protonated protein samples in solid state NMR

Determination of methyl order parameters using solid state NMR under off magic angle spinning

Accurate Determination of 1 H‐ 15 N Dipolar Couplings Using Inaccurate Settings of the Magic Angle in Solid‐State NMR Spectroscopy

Accurate Determination of 1 H‐ 15 N Dipolar Couplings Using Inaccurate Settings of the Magic Angle in Solid‐State NMR Spectroscopy

Overcoming Volume Selectivity of Dipolar Recoupling in Biological Solid‐State NMR Spectroscopy

Overcoming Volume Selectivity of Dipolar Recoupling in Biological Solid‐State NMR Spectroscopy

Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins

Long‐Lived States to Monitor Protein Unfolding by Proton NMR

Cover Picture: Long‐Lived States to Monitor Protein Unfolding by Proton NMR (ChemPhysChem 15/2011)

Berichtigung: Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization

Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization †

Corrigendum: Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization

Scavenging Free Radicals To Preserve Enhancement and Extend Relaxation Times in NMR using Dynamic Nuclear Polarization †

Long‐lived States in Multiple‐Spin Systems

Measurement of Slow Diffusion Coefficients of Molecules with Arbitrary Scalar Couplings via Long‐Lived Spin States

Extending the Scope of Singlet‐State Spectroscopy