Polypeptide Conjugate Binders for Protein Recognition

2007 ◽  
pp. 89-106 ◽  
Author(s):  
Lars Baltzer
Keyword(s):  
Protein Recognition

scholarly journals Discrimination of deletion to point cytokine mutants based on an array of cross-reactive receptors mimicking protein recognition by heparan sulfate

2021 ◽  
Author(s):  
Maria Genua ◽  
Laurie-Amandine Garçon ◽  
Yulia N. Sergeeva ◽  
Els Saesen ◽  
Benjamin Musnier ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Protein Recognition

Ligand Specificity of CS-35, a Monoclonal Antibody That Recognizes Mycobacterial Lipoarabinomannan:  A Model System for Oligofuranoside−Protein Recognition

2007 ◽  
Vol 129 (34) ◽  
pp. 10489-10502 ◽  
Author(s):  
Christoph Rademacher ◽  
Glen K. Shoemaker ◽  
Hyo-Sun Kim ◽  
Ruixiang Blake Zheng ◽  
Hashem Taha ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Model System ◽  
Protein Recognition ◽  
Ligand Specificity

scholarly journals Identification of Protein Recognition Elements within Heparin Chains Using Enzymatic Foot-Printing in Solution and Online SEC/MS

2020 ◽  
Vol 92 (11) ◽  
pp. 7565-7573 ◽  
Author(s):  
Chendi Niu ◽  
Yunlong Zhao ◽  
Cedric E. Bobst ◽  
Sergey N. Savinov ◽  
Igor A. Kaltashov
Keyword(s):  
Protein Recognition ◽  
Recognition Elements

Molecular imprinting of proteins emerging as a tool for protein recognition

2008 ◽  
Vol 6 (14) ◽  
pp. 2459 ◽  
Author(s):  
Toshifumi Takeuchi ◽  
Takayuki Hishiya
Keyword(s):  
Molecular Imprinting ◽  
Protein Recognition

Molecularly imprinted fluorescent and colorimetric sensor based on TiO2@Cu(OH)2 nanoparticle autocatalysis for protein recognition

2013 ◽  
Vol 1 (9) ◽  
pp. 1256 ◽  
Author(s):  
Yanxia Li ◽  
Yujun Li ◽  
Lihua Huang ◽  
Qiu Bin ◽  
Zhenyu Lin ◽  
...  
Keyword(s):  
Colorimetric Sensor ◽  
Protein Recognition ◽  
Molecularly Imprinted

scholarly journals Conformation and protein interactions of intramolecular DNA and phosphorothioate four-way junctions

2020 ◽  
pp. 153537022097397
Author(s):  
Maria Troisi ◽  
Mitchell Klein ◽  
Andrew C Smith ◽  
Gaston Moorhead ◽  
Yonatan Kebede ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Therapeutic Potential ◽  
Dnase I ◽  
Protein Recognition ◽  
Exonuclease Iii ◽  
Branched Dna ◽  
Acid Cleavage ◽  
Nuclease Digestion ◽  
Nuclease Resistance ◽  
Exo Iii

The objectives of this study are to evaluate the structure and protein recognition features of branched DNA four-way junctions in an effort to explore the therapeutic potential of these molecules. The classic immobile DNA 4WJ, J1, is used as a matrix to design novel intramolecular junctions including natural and phosphorothioate bonds. Here we have inserted H2-type mini-hairpins into the helical termini of the arms of J1 to generate four novel intramolecular four-way junctions. Hairpins are inserted to reduce end fraying and effectively eliminate potential nuclease binding sites. We compare the structure and protein recognition features of J1 with four intramolecular four-way junctions: i-J1, i-J1(PS1), i-J1(PS2) and i-J1(PS3). Circular dichroism studies suggest that the secondary structure of each intramolecular 4WJ is composed predominantly of B-form helices. Thermal unfolding studies indicate that intramolecular four-way junctions are significantly more stable than J1. The Tm values of the hairpin four-way junctions are 25.2° to 32.2°C higher than the control, J1. With respect to protein recognition, gel shift assays reveal that the DNA-binding proteins HMGBb1 and HMGB1 bind the hairpin four-way junctions with affinity levels similar to control, J1. To evaluate nuclease resistance, four-way junctions are incubated with DNase I, exonuclease III (Exo III) and T5 exonuclease (T5 Exo). The enzymes probe nucleic acid cleavage that occurs non-specifically (DNase I) and in a 5ʹ→3ʹ (T5 Exo) and 3ʹ→5ʹ direction (Exo III). The nuclease digestion assays clearly show that the intramolecular four-way junctions possess significantly higher nuclease resistance than the control, J1.

α-Man monolayer formation via Si–C bond formation and protein recognition

2009 ◽  
Vol 518 (2) ◽  
pp. 699-702 ◽  
Author(s):  
Koji Funato ◽  
Naoto Shirahata ◽  
Yoshiko Miura
Keyword(s):  
Bond Formation ◽  
Protein Recognition ◽  
Monolayer Formation

scholarly journals Behavioral Responses of Phormia regina (Meigen) to Labellar Stimulation with Amino Acids

1973 ◽  
Vol 61 (1) ◽  
pp. 74-88 ◽  
Author(s):  
Nancy R. Goldrich
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Behavioral Responses ◽  
Behavioral Data ◽  
Phormia Regina ◽  
Protein Recognition ◽  
Electrophysiological Investigation ◽  
Nutritional Information ◽  
Electrophysiological Responses

Behavioral responses to labellar stimulation with 19 L-amino acids were predicted on the basis of electrophysiological responses of largest labellar hairs. With the exceptions alanine, aspartic and glutamic acids, and valine tests of these predictions confirmed that Phormia can discriminate amino acids, and that these acids may be grouped according to their effects. Electrophysiological investigation of the four exceptions was repeated and results were consistent with the behavioral data. In particular, these acids elicited previously unreported responses from the salt receptor. The discrepancies between this and earlier studies may be explainable, in part, on methodological grounds. There was evidence for response differences among hairs of different sizes and among the largest labellar hairs themselves. The significance of amino acid discrimination for the problem of protein recognition can only be speculated upon until more complete electrophysiological and nutritional information is available.

Sign in / Sign up

Export Citation Format

Share Document