scholarly journals Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association.

1995 ◽  
Vol 95 (4) ◽  
pp. 1553-1560 ◽  
Author(s):  
D A Wilcox ◽  
C M Paddock ◽  
S Lyman ◽  
J C Gill ◽  
P J Newman
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Calcium Binding ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Amino Terminus ◽  
Integrin Subunit ◽  
Glanzmann Thrombasthenia ◽  
Binding Domains

The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution

FEBS Letters ◽  
1995 ◽  
Vol 372 (1) ◽  
pp. 96-98 ◽  
Author(s):  
Markus Linder ◽  
Gunnar Lindeberg ◽  
Tapani Reinikainen ◽  
Tuula T. Teeri ◽  
Göran Pettersson
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Binding Domains ◽  
The Difference ◽  
Cellulose Binding

scholarly journals Governing the monomer-dimer ratio of human cystatin c by single amino acid substitution in the hinge region.

2009 ◽  
Vol 56 (3) ◽  
Author(s):  
Aneta Szymańska ◽  
Adrianna Radulska ◽  
Paulina Czaplewska ◽  
Anders Grubb ◽  
Zbigniew Grzonka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cystatin C ◽  
Amino Acid Substitution ◽  
Mutational Analysis ◽  
Three Dimensional ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Human Cystatin C ◽  
Human Cystatin

Three dimensional domain swapping is one of the mechanisms involved in formation of insoluble aggregates of some amyloidogenic proteins. It has been proposed that proteins able to swap domains may share some common structural elements like conformationally constrained flexible turns/loops. We studied the role of loop L1 in the dimerization of human cystatin C using mutational analysis. Introduction of turn-favoring residues such as Asp or Asn into the loop sequence (in position 57) leads to a significant reduction of the dimer fraction in comparison with the wild type protein. On the other hand, introduction of a proline residue in position 57 leads to efficient dimer formation. Our results confirm the important role of the loop L1 in the dimerization process of human cystatin C and show that this process can be to some extent governed by single amino acid substitution.

scholarly journals A large compressibility change of protein induced by a single amino acid substitution

1996 ◽  
Vol 5 (3) ◽  
pp. 542-545 ◽  
Author(s):  
Kunihiko Gekko ◽  
Youjiro Tamura ◽  
Eiji Ohmae ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid

scholarly journals A single amino acid substitution in the Ω-like loop of E. coli PBP5 disrupts its ability to maintain cell shape and intrinsic beta-lactam resistance

Microbiology ◽  
2015 ◽  
Vol 161 (4) ◽  
pp. 895-902 ◽  
Author(s):  
Mouparna Dutta ◽  
Debasish Kar ◽  
Ankita Bansal ◽  
Sandeep Chakraborty ◽  
Anindya S. Ghosh
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Cell Shape ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Beta Lactam ◽  
E Coli
Sign in / Sign up

Export Citation Format

Share Document