P
Peter Nollert
Researcher at Emerald Group Publishing
Publications - 40
Citations - 4510
Peter Nollert is an academic researcher from Emerald Group Publishing. The author has contributed to research in topics: Crystallization & Bacteriorhodopsin. The author has an hindex of 24, co-authored 40 publications receiving 4369 citations. Previous affiliations of Peter Nollert include Technische Universität München & deCODE genetics.
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Journal ArticleDOI
Structure of a glycerol-conducting channel and the basis for its selectivity.
Daxiong Fu,Andrew Libson,Larry J. W. Miercke,Weitzman C,Peter Nollert,J. Krucinski,Robert M. Stroud +6 more
TL;DR: The crystal structure of the Escherichia coli glycerol facilitator (GlpF) elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded.
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Control of the selectivity of the aquaporin water channel family by global orientational tuning.
Emad Tajkhorshid,Peter Nollert,Morten Østergaard Jensen,Larry J. W. Miercke,Joseph D. O'Connell,Robert M. Stroud,Klaus Schulten +6 more
TL;DR: Aquaporins are transmembrane channels found in cell membranes of all life forms and their apparently paradoxical property, facilitation of efficient permeation of water while excluding protons, is examined.
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Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution
Hassan Belrhali,Peter Nollert,Antoine Royant,Christoph Menzel,Jurg P. Rosenbusch,Ehud M. Landau,Eva Pebay-Peyroula +6 more
TL;DR: The structure of protein, lipid and water molecules in the crystals represents the functional entity of bR in the purple membrane of the bacteria at atomic resolution.
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High Resolution X-Ray Structure of an Early Intermediate in the Bacteriorhodopsin Photocycle
Karl Edman,Peter Nollert,Peter Nollert,Antoine Royant,Antoine Royant,Hassan Belrhali,Eva Pebay-Peyroula,Janos Hajdu,Richard Neutze,Ehud M. Landau +9 more
TL;DR: The high-resolution X-ray structure of an early intermediate in the photocycle of bacteriorhodopsin is described, which is formed directly after photoexcitation.
Journal ArticleDOI
X-Ray Structure of Sensory Rhodopsin II at 2.1 A Resolution
Antoine Royant,Peter Nollert,Peter Nollert,Karl Edman,Richard Neutze,Ehud M. Landau,Eva Pebay-Peyroula,Javier Navarro +7 more
TL;DR: The high-resolution structure of pSRII provides a structural basis to elucidate the mechanisms of phototransduction and color tuning and reveals a putative chloride ion that is coupled to the Schiff base by means of a hydrogen-bond network and a unique, positively charged surface patch for a probable interaction with HtrII.