Characterization of DLC1-SAM Equilibrium Unfolding at the Amino Acid Residue Level

Biochemistry ◽  
2009 ◽  
Vol 48 (19) ◽  
pp. 4040-4049 ◽  
Author(s):  
Shuai Yang ◽  
Christian G. Noble ◽  
Daiwen Yang
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Residue Level ◽  
Equilibrium Unfolding

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

scholarly journals Roles of membrane transporters: connecting the dots from sequence to phenotype

2019 ◽  
Vol 124 (2) ◽  
pp. 201-208 ◽  
Author(s):  
Rakesh David ◽  
Caitlin S Byrt ◽  
Stephen D Tyerman ◽  
Matthew Gilliham ◽  
Stefanie Wege
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Membrane Transporters ◽  
Plant Performance ◽  
Single Amino Acid ◽  
Physiological Data ◽  
Data Sets ◽  
Single Amino Acid Residue ◽  
The Impact

Abstract Background Plant membrane transporters are involved in diverse cellular processes underpinning plant physiology, such as nutrient acquisition, hormone movement, resource allocation, exclusion or sequestration of various solutes from cells and tissues, and environmental and developmental signalling. A comprehensive characterization of transporter function is therefore key to understanding and improving plant performance. Scope and Conclusions In this review, we focus on the complexities involved in characterizing transporter function and the impact that this has on current genomic annotations. Specific examples are provided that demonstrate why sequence homology alone cannot be relied upon to annotate and classify transporter function, and to show how even single amino acid residue variations can influence transporter activity and specificity. Misleading nomenclature of transporters is often a source of confusion in transporter characterization, especially for people new to or outside the field. Here, to aid researchers dealing with interpretation of large data sets that include transporter proteins, we provide examples of transporters that have been assigned names that misrepresent their cellular functions. Finally, we discuss the challenges in connecting transporter function at the molecular level with physiological data, and propose a solution through the creation of new databases. Further fundamental in-depth research on specific transport (and other) proteins is still required; without it, significant deficiencies in large-scale data sets and systems biology approaches will persist. Reliable characterization of transporter function requires integration of data at multiple levels, from amino acid residue sequence annotation to more in-depth biochemical, structural and physiological studies.

scholarly journals Genetic Characterization of Resistance to Extended-Spectrum β-Lactams in Klebsiella oxytoca Isolates Recovered from Patients with Septicemia at Hospitals in the Stockholm Area

1999 ◽  
Vol 43 (5) ◽  
pp. 1294-1297 ◽  
Author(s):  
Shang Wei Wu ◽  
Kathrine Dornbusch ◽  
Göran Kronvall
Keyword(s):  
Amino Acid ◽  
Dna Sequencing ◽  
Amino Acid Residue ◽  
Genetic Characterization ◽  
Consensus Sequence ◽  
Klebsiella Oxytoca ◽  
Clinical Isolates ◽  
Amino Acid Residues ◽  
Lactamase Gene

ABSTRACT Two β-lactamase gene regions were characterized by DNA sequencing in eight clinical isolates of Klebsiella oxytoca. Thebla OXY-2a region encoded a β-lactamase nearly identical to OXY-2 (one amino acid residue substituted) and conferred aztreonam and cefuroxime resistance on the K. oxytoca isolates. Overproduction of OXY-2a was caused by a G-to-A substitution of the fifth nucleotide in the −10 consensus sequence ofbla OXY-2a. Thebla OXY-1a was identified in a susceptible strain, and the OXY-1a enzyme differed from OXY-1 by two amino acid residues.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

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