2001 - Fellow of Alfred P. Sloan Foundation
Harald Schwalbe focuses on Crystallography, Nuclear magnetic resonance spectroscopy, Biochemistry, RNA and Stereochemistry. The various areas that he examines in his Crystallography study include Dihedral angle, Heteronuclear molecule, Resonance and Lysozyme. Harald Schwalbe interconnects Chemical physics, Solid-state nuclear magnetic resonance, Photodissociation, Homonuclear molecule and Protein structure in the investigation of issues within Nuclear magnetic resonance spectroscopy.
Biochemistry is frequently linked to Mycobacterium tuberculosis in his study. His work carried out in the field of RNA brings together such families of science as Folding, Molecular biology, Base pair and Nucleic acid. Harald Schwalbe has researched Stereochemistry in several fields, including Tripeptide, Phenylalanine, Polyproline helix, DNA and Membrane protein.
His main research concerns Nuclear magnetic resonance spectroscopy, Crystallography, Stereochemistry, RNA and Biochemistry. His Nuclear magnetic resonance spectroscopy research incorporates themes from Folding, Two-dimensional nuclear magnetic resonance spectroscopy and Analytical chemistry. The Crystallography study combines topics in areas such as Dihedral angle, Lysozyme, Protein folding, Protein structure and Chemical shift.
The study incorporates disciplines such as Amino acid, Polyproline helix and G-quadruplex, Oligonucleotide, DNA in addition to Stereochemistry. His studies deal with areas such as Base pair, Nucleic acid, Computational biology and Protein secondary structure as well as RNA. His study in Riboswitch is interdisciplinary in nature, drawing from both Biophysics, Cobalamin riboswitch, Aptamer and Ligand.
His primary areas of study are RNA, Nuclear magnetic resonance spectroscopy, Biophysics, Stereochemistry and Computational biology. His RNA study combines topics in areas such as Crystallography, Viral replication and Protein secondary structure. Harald Schwalbe brings together Crystallography and Motif to produce work in his papers.
Harald Schwalbe is interested in Heteronuclear molecule, which is a branch of Nuclear magnetic resonance spectroscopy. His research on Biophysics also deals with topics like
His scientific interests lie mostly in RNA, Biophysics, Nuclear magnetic resonance spectroscopy, Riboswitch and Computational biology. The concepts of his RNA study are interwoven with issues in Protein tertiary structure, Polymerase, Stereochemistry and Protein secondary structure. His work deals with themes such as Nucleobase, Crystallography, Druggability, Acridine and Binding selectivity, which intersect with Protein tertiary structure.
His Crystallography study combines topics from a wide range of disciplines, such as Nucleic acid structure and Two-dimensional nuclear magnetic resonance spectroscopy. His Biophysics research is multidisciplinary, relying on both Plasma protein binding, Transcription factor, Transcription and In vitro. Harald Schwalbe undertakes interdisciplinary study in the fields of Nuclear magnetic resonance spectroscopy and Cell studies through his works.
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Long-Range Interactions Within a Nonnative Protein
Judith Klein-Seetharaman;Maki Oikawa;Shaun B. Grimshaw;Julia Wirmer.
Science (2002)
NMR Spectroscopy of RNA
Boris Fürtig;Christian Richter;Jens Wöhnert;Harald Schwalbe.
ChemBioChem (2003)
Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations.
Lorna J. Smith;Kimberly A. Bolin;Harald Schwalbe;Malcolm W. MacArthur.
Journal of Molecular Biology (1996)
Perspectives on NMR in drug discovery: a technique comes of age
Maurizio Pellecchia;Ivano Bertini;David Cowburn;Claudio Dalvit.
Nature Reviews Drug Discovery (2008)
The concept of a random coil: Residual structure in peptides and denatured proteins
Lorna J. Smith;Klaus M. Fiebig;Harald Schwalbe;Christopher M. Dobson.
Folding and Design (1996)
Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.
Harald Schwalbe;Klaus M. Fiebig;Matthias Buck;Jonathan A. Jones.
Biochemistry (1997)
Mechanistic insight from the crystal structure of mitochondrial complex I
Volker Zickermann;Christophe Wirth;Hamid Nasiri;Hamid Nasiri;Karin Siegmund.
Science (2015)
Structure and dynamics of the homologous series of alanine peptides: a joint molecular dynamics/NMR study.
Jürgen Graf;Phuong H. Nguyen;Gerhard Stock;Harald Schwalbe.
Journal of the American Chemical Society (2007)
Discovery of protein phosphatase inhibitor classes by biology-oriented synthesis
Andrea Nören-Müller;Ivan Reis-Corrêa;Heino Prinz;Claudia Rosenbaum.
Proceedings of the National Academy of Sciences of the United States of America (2006)
NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Bettina Elshorst;Mirko Hennig;Holger Försterling;Alexander Diener.
Biochemistry (1999)
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