R
Robert Huber
Researcher at Technische Universität München
Publications - 742
Citations - 76282
Robert Huber is an academic researcher from Technische Universität München. The author has contributed to research in topics: Active site & Protein structure. The author has an hindex of 139, co-authored 671 publications receiving 73557 citations. Previous affiliations of Robert Huber include Munich University of Applied Sciences & Russian Academy of Sciences.
Papers
More filters
Journal ArticleDOI
Functional significance of flexibility in proteins
Robert Huber,W. S. Bennett +1 more
TL;DR: The structural basis and the functional implications of large‐scale flexibility are discussed for three systems: trypsin–trypsinogen, immunoglobulins, and citrate synthase.
Journal ArticleDOI
Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin.
A. Van De Locht,Doriano Lamba,Margit Bauer,Robert Huber,T. Friedrich,B Kröger,W. Höffken,Wolfram Bode +7 more
TL;DR: The tight (Ki = 2 × 10(‐13) M) binding of rhodniin to thrombin is the result of the sum of steric and charge complementarity of the amino‐terminal domain towards the active‐site cleft, and of the electrostatic interactions between the carboxy‐ terminal domain and the exosite.
Journal ArticleDOI
Omnidirectional spin-wave nanograting coupler
TL;DR: The magnonic grating coupler is found to be more versatile compared with gratings in photonics and plasmonics, and allows one to convert, in particular, straight microwave antennas into omnidirectional emitters for short-wavelength spin waves, which are key to cellular nonlinear networks and integrated magnonics.
Journal ArticleDOI
Crystal structure of cathepsin b inhibited with ca030 at 2.0-a resolution : a basis for the design of specific epoxysuccinyl inhibitors
TL;DR: The structure confirms the role of residues His 110 and His 111 as the receptors of a peptidic substrate C-terminal carboxylic group and suggests that an epoxysuccinyl fragment can be used to extend binding into primed and nonprimed substrate binding sites of a papain-like cysteine protease.
Journal ArticleDOI
Pyrobaculum gen. nov., a new genus of neutrophilic, rod-shaped archaebacteria from continental solfataras growing optimally at 100°C
TL;DR: Seven members of a new group of rod-shaped hyperthermophilic neutrophilic archaebacteria were isolated from boiling neutral to alkaline solfataric waters from the Azores, Iceland, and Italy, representing a new genus which is named Pyrobaculum (the “fire stick”).