Book synopsis: This book presents a survey of recent developments in protein biochemistry. Top researchers in the field of protein biochemistry describe modern methods to address the challenges of protein purification by three-phase partitioning, and their folding and degradation by the functions of chaperones. The significance of peptide purity for fibril formation is addressed as well as the use of target oriented peptide arrays in palliative approaches in mucoviszidose. The design and application of protein epitope mimetics just as the structural resolving of the misfolding of various mutant proteins in serpinopathies enlarge our tools in resolving pathophysiological imbalances
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
Conserpin is an engineered protein that represents the consensus of a sequence alignment of eukaryot...
The hepatic secretory protein a1-antitrypsin, a member of the serpin family of serine proteinase inh...
Book synopsis: This book presents a survey of recent developments in protein biochemistry. Top resea...
Tschesche H, ed. Methods in Protein Biochemistry. Berlin: DeGruyter; 2011.This book presents a surve...
Protein misfolding is associated with a range of diseases and occurs when a protein meanders from it...
Proteins are biopolymers that present the particularity to adopt a specific tridimensional structure...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
α1-Antitrypsin is the prototypical member of the serine proteinase inhibitor or serpin superfamily o...
The common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that are reta...
Protein folding is the process by which a polypeptide chain acquires its functional, native 3D struc...
Point mutations cause members of the serine protease inhibitor (serpin) superfamily to undergo a nov...
AbstractSerine proteinase inhibitors (Serpins) are irreversible suicide inhibitors of proteases that...
AbstractThe common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that ...
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
Conserpin is an engineered protein that represents the consensus of a sequence alignment of eukaryot...
The hepatic secretory protein a1-antitrypsin, a member of the serpin family of serine proteinase inh...
Book synopsis: This book presents a survey of recent developments in protein biochemistry. Top resea...
Tschesche H, ed. Methods in Protein Biochemistry. Berlin: DeGruyter; 2011.This book presents a surve...
Protein misfolding is associated with a range of diseases and occurs when a protein meanders from it...
Proteins are biopolymers that present the particularity to adopt a specific tridimensional structure...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
α1-Antitrypsin is the prototypical member of the serine proteinase inhibitor or serpin superfamily o...
The common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that are reta...
Protein folding is the process by which a polypeptide chain acquires its functional, native 3D struc...
Point mutations cause members of the serine protease inhibitor (serpin) superfamily to undergo a nov...
AbstractSerine proteinase inhibitors (Serpins) are irreversible suicide inhibitors of proteases that...
AbstractThe common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that ...
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
Conserpin is an engineered protein that represents the consensus of a sequence alignment of eukaryot...
The hepatic secretory protein a1-antitrypsin, a member of the serpin family of serine proteinase inh...