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Prediction of chain flexibility in proteins
This work has analyzed 31 refined protein structures to develop a method for predicting flexible segments from a given amino acid sequence and found that segmental flexibility is more indicative of an antigenic determinant than the selection criteria mentioned above. Expand
Structure of the outer membrane protein A transmembrane domain
The structure of the OmpA transmembrane domain consists of a regular, extended eight-stranded ß-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Expand
Principles of Protein Structure
1 Amino Acids.- 1.1 The 20 Standard Amino Acids.- 1.2 Why Were Just These Amino Acids Selected?.- 1.3 Colinear Relation Between Nucleic Acids and Polypeptides.- 1.4 Side Chain Properties.- 1.5Expand
The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence.
The OmpX structure shows that within a family of virulence-related membrane proteins, the membrane-spanning part of the protein is much better conserved than the extracellular loops. Expand
Structural Basis for the Entrance into the Phenylpropanoid Metabolism Catalyzed by Phenylalanine Ammonia-Lyase
The enzyme from parsley was crystallized, and the structure was elucidated at 1.7-Å resolution, and a pathway of the catalyzed reaction is proposed in agreement with established biochemical data. Expand
The structure of bacterial outer membrane proteins.
  • G. Schulz
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 11 October 2002
The beta-barrels are suitable objects for channel engineering, because the structures are simple and because many of these proteins can be produced into inclusion bodies and recovered therefrom in the exact native conformation. Expand
Structure and function of a squalene cyclase.
The crystal structure of squalene-hopene cyclase from Alicyclobacillus acidocaldarius was determined and reveals a membrane protein with membrane-binding characteristics similar to those of prostaglandin-H2 synthase, the only other reported protein of this type. Expand
β-Barrel membrane proteins
Abstract β-Barrel proteins are found in the outer membranes of bacteria, mitochondria and chloroplasts. The presently known sizes range from small eight-stranded to large twenty-two-stranded βExpand
Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
The crystal structures of the catalytic fragment of chicken poly(ADP-ribose) polymerase with and without a nicotinamide-analogue inhibitor have been elucidated, because this enzyme is involved in the regulation of DNA repair, its inhibitors are of interest for cancer therapy. Expand
The Structure of a Mycobacterial Outer-Membrane Channel
An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel, the first structure of a mycobacterial outer-membrane protein. Expand