scholarly journals Primary structure of the "hinge" region of human IgG3. Probable quadruplication of a 15-amino acid residue basic unit.

1977 ◽  
Vol 252 (3) ◽  
pp. 883-889
Author(s):  
T E Michaelsen ◽  
B Frangione ◽  
E C Franklin
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Primary Structure ◽  
Hinge Region ◽  
Basic Unit

Primary structure polymorphism at amino acid residue 72 of human p53

1987 ◽  
Vol 7 (2) ◽  
pp. 961-963
Author(s):  
G J Matlashewski ◽  
S Tuck ◽  
D Pim ◽  
P Lamb ◽  
J Schneider ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Residue ◽  
Primary Structure ◽  
Transformed Cells ◽  
Genomic Clones

We analyzed p53 cDNA and genomic clones from a variety of normal and transformed cells. Sequence analysis of these clones revealed that amino acid residue 72 can be an arginine, proline, or cysteine. This single codon difference results in electrophoretically distinct forms of human p53 seen in normal and transformed cells.

scholarly journals PHYTOHEMAGGLUTININ MITOGENIC PROTEINS

1973 ◽  
Vol 138 (4) ◽  
pp. 939-951 ◽  
Author(s):  
J. Bruce Miller ◽  
Claudia Noyes ◽  
Robert Heinrikson ◽  
Henry S. Kingdon ◽  
Stanley Yachnin
Keyword(s):  
Amino Acid ◽  
Phaseolus Vulgaris ◽  
Amino Acid Residue ◽  
Primary Structure ◽  
Biological Activities ◽  
Amino Acid Sequences ◽  
Structural Basis ◽  
Amino Terminal ◽  
Isoelectric Points

The phytohemagglutinin (PHAP) glycoproteins derived from Phaseolus vulgaris consist of five isomitogens that are tetrameric structures made up of two different glycoprotein subunits. Although identical in size (mol wt = 34,000), the subunits differ in their isoelectric points and amino acid sequences for six of the first seven amino-terminal residues, but are identical in primary structure from the 8th through the 24th amino acid residue. The isomitogen containing four L subunits (L-PHAP) is a potent leukoagglutinin and mitogen that lacks hemagglutinating properties. The isomitogen made up of four R subunits (4R H-PHAP) is a potent hemagglutinin. The hybrid isomitogens consisting of varying proportions of the two subunits (3L-1R, 2L-2R, 1L-3R) are capable of causing mixed erythrocyte-lymphocyte agglutination. These studies provide a structural basis for explaining the differences in biological activities of the various PHAP isomitogens.

scholarly journals Primary structure polymorphism at amino acid residue 72 of human p53.

1987 ◽  
Vol 7 (2) ◽  
pp. 961-963 ◽  
Author(s):  
G J Matlashewski ◽  
S Tuck ◽  
D Pim ◽  
P Lamb ◽  
J Schneider ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Residue ◽  
Primary Structure ◽  
Transformed Cells ◽  
Genomic Clones

We analyzed p53 cDNA and genomic clones from a variety of normal and transformed cells. Sequence analysis of these clones revealed that amino acid residue 72 can be an arginine, proline, or cysteine. This single codon difference results in electrophoretically distinct forms of human p53 seen in normal and transformed cells.

scholarly journals Amino Acid Residue at the 165th Position Tunes Eyfp Chromophore Maturation. A Structure-Based Design

2021 ◽  
Author(s):  
Nadya V. Pletneva ◽  
Eugene G. Maksimov ◽  
Elena A. Protasova ◽  
Anastasia V. Mamontova ◽  
Tatiana R. Simonyan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue
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