Microenvironments of Basic Amino Acids in Amphipathic .alpha.-Helixes Bound to Phospholipid: 13C NMR Studies Using Selectively Labeled Peptides

Biochemistry ◽  
1995 ◽  
Vol 34 (28) ◽  
pp. 9219-9226 ◽  
Author(s):  
Sissel Lund-Katz ◽  
Michael C. Phillips ◽  
Vinod K. Mishra ◽  
Jere P. Segrest ◽  
G. M. Anantharamaiah
Keyword(s):  
Amino Acids ◽  
13C Nmr ◽  
Nmr Studies ◽  
Basic Amino Acids

scholarly journals Investigation of exponential RNA amplification by the Qβ replicase complex

2014 ◽  
Vol 70 (a1) ◽  
pp. C1602-C1602
Author(s):  
Heidi Olesen ◽  
Charlotte Knudsen ◽  
Paulina Seweryn ◽  
Ditlev Brodersen ◽  
Zarina Kutlubaeva ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nmr Spectroscopy ◽  
Rna Virus ◽  
Β Subunit ◽  
Rna Amplification ◽  
Nmr Studies ◽  
Basic Amino Acids ◽  
Rna Backbone

Positive-stranded RNA viruses are common among human pathogenic viruses, which often cooperate with host proteins to fulfill essential functions during infection. One function is replication of the viral genome. The Qβ phage is a positive-stranded RNA virus that infects E.coli. The Qβ replicase holo enzyme comprises the phage-encoded RNA-dependent RNA polymerase (β-subunit) and the host-encoded translation elongation factors, EF-Ts and EF-Tu as well as the ribosomal protein S1. The Qβ replicase has an extraordinary ability to exponentially amplify RNA in vivo and in vitro. A prerequisite for this is release of product and template RNA as single strands that can serve as new templates in subsequent rounds of replication. The role of S1 in the Qβ replicase is not clear. Recently, S1 was found to promote release of single-stranded product in Qβ replicase–mediated RNA synthesis. We have undertaken NMR spectroscopy and crystallization trials to improve our understanding of distinct S1 domains in solution as well as the ribosome- and replicase-binding properties of S1. Expression of distinct S1 domains for NMR spectroscopy has been optimized by use of autoinduction and results in high yields of [13C15N]-labelled protein fragments. These have proven very suitable for NMR studies and spectra revealed both ordered and disordered regions in the protein. Studies are ongoing. The structure of the Qβ core complex was recently determined at 2.5Å resolution. Thus, co-crystallization of the Qβ core in complex with S1 domains was undertaken and different crystal forms were obtained. These initial crystals diffracted to 3.2Å resolution and data processing as well as further optimization of the crystals is ongoing. S1 is thought to bind the β-subunit close to a region lined with basic amino acids, which potentially could facilitate interactions with the template RNA backbone and split it from the product strand. We demonstrate that neutralization of these basic amino acids indeed decrease or abolish infectivity of the Qβ phage. However, only one mutation, R503A affects the exponential replication in vitro. Crystallization of the Qβ holo enzyme bound to a truncated legitimate RNA template will be the next step for investigation of the mechanism of exponential RNA amplification by Qβ replicase.

Interfacial basic amino acids increase the lipid affinity of class A amphipathic helix: Evidence for snorkel hypothesis by 13C-NMR spectroscopy

Peptides ◽  
1994 ◽  
pp. 370-372
Author(s):  
S. Lund-Katz ◽  
M.C. Phillips ◽  
V.K. Mishra ◽  
Y.V. Venkatachalapathi ◽  
J.P. Segrest ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nmr Spectroscopy ◽  
13C Nmr ◽  
13C Nmr Spectroscopy ◽  
Amphipathic Helix ◽  
Basic Amino Acids ◽  
Class A

Does the polyamine carrier system absorb basic amino acids?

2001 ◽  
Vol 120 (5) ◽  
pp. A142-A142
Author(s):  
J GASKEY ◽  
E SEIDEL
Keyword(s):  
Amino Acids ◽  
Carrier System ◽  
Basic Amino Acids

scholarly journals In vivo 13C NMR studies of glucose catabolism by isolated rumen bacteria

1989 ◽  
Vol 29 (1) ◽  
pp. 83-88 ◽  
Author(s):  
J. P. Grivet ◽  
J. Stevani ◽  
G. Hannequart ◽  
M. Durand
Keyword(s):  
13C Nmr ◽  
Rumen Bacteria ◽  
Nmr Studies ◽  
Glucose Catabolism

Atypical amino acids inhibit histidine, valine, or lysine transport into rat brain

1983 ◽  
Vol 245 (4) ◽  
pp. R556-R563 ◽  
Author(s):  
J. K. Tews ◽  
A. E. Harper
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Blood Brain Barrier ◽  
Brain Slices ◽  
Aromatic Amino Acids ◽  
Brain Barrier ◽  
Basic Amino Acids ◽  
Large Neutral Amino Acids ◽  
Neutral Amino Acids ◽  
Single Meal

Transport of histidine, valine, or lysine into rat brain slices and across the blood-brain barrier (BBB) was determined in the presence of atypical nonprotein amino acids. Competitors of histidine and valine transport in slices were large neutral amino acids including norleucine, norvaline, alpha-aminooctanoate, beta-methylphenylalanine, and alpha-aminophenylacetate. Less effective were aromatic amino acids with ring substituents; ineffective were basic amino acids and omega-amino isomers of norleucine and aminooctanoate. Lysine transport was moderately depressed by homoarginine or ornithine plus arginine; large neutral amino acids were also similarly inhibitory. Histidine or valine transport across the BBB was also strongly inhibited by large neutral amino acids that were the most effective competitors in the slices (norvaline, norleucine, alpha-aminooctanoate, and alpha-aminophenylacetate); homoarginine and 8-aminooctanoate were ineffective. Homoarginine, ornithine, and arginine almost completely blocked lysine transport, but the large neutral amino acids were barely inhibitory. When rats were fed a single meal containing individual atypical large neutral amino acids or homoarginine, brain pools of certain large neutral amino acids or of arginine and lysine, respectively, were depleted.

scholarly journals Structural Investigations of C-Nitrosobenzenes. Part 3.1 Solid-state and Solution 13C NMR Studies, and Crystal Structure of E-(4-CIC6H4NO)2

1999 ◽  
Vol 23 (3) ◽  
pp. 202-203
Author(s):  
Daniel A. Fletcher ◽  
Brian G. Gowenlock ◽  
Keith G. Orrell ◽  
David C. Apperley ◽  
Michael B. Hursthouse ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Solid State ◽  
13C Nmr ◽  
Nmr Studies ◽  
Structural Investigations ◽  
Nmr Data ◽  
C Nmr

Solid-state and solution 13C NMR data for the monomers and dimers of 3- and 4-substituted nitrosobenzenes, and the crystal structure of E-(4-CIC6H4NO)2 are reported.

scholarly journals THE BASIC AMINO ACIDS OF WOOL

1930 ◽  
Vol 86 (1) ◽  
pp. 107-111
Author(s):  
Hubert Bradford Vickery ◽  
Richard J. Block
Keyword(s):  
Amino Acids ◽  
Basic Amino Acids
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