Search Results - "Garcia Seisdedos, Hector"
-
1
Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering
Published in Angewandte Chemie International Edition (16-04-2019)“…Mutations and changes in a protein's environment are well known for their potential to induce misfolding and aggregation, including amyloid formation…”
Get full text
Journal Article -
2
Symmetry Breaking in Homo-Oligomers: The Curious Case of Mega-Hemocyanin
Published in Structure (London) (06-01-2015)“…Mega-hemocyanin is a 13.5 MDa oxygen transporter found in snails. It is built from three stacked rings involving ten subunits each. The cryo-EM structure of…”
Get full text
Journal Article -
3
Mutant libraries reveal negative design shielding proteins from supramolecular self-assembly and relocalization in cells
Published in Proceedings of the National Academy of Sciences - PNAS (01-02-2022)“…Understanding the molecular consequences of mutations in proteins is essential to map genotypes to phenotypes and interpret the increasing wealth of genomic…”
Get full text
Journal Article -
4
Active site center redesign increases protein stability preserving catalysis in thioredoxin
Published in Protein science (01-09-2022)“…The stabilization of natural proteins is a long‐standing desired goal in protein engineering. Optimizing the hydrophobicity of the protein core often results…”
Get full text
Journal Article -
5
Infinite Ansammlungen gefalteter Proteine im Kontext von Evolution, Krankheiten und Proteinentwicklung
Published in Angewandte Chemie (16-04-2019)“…Mutationen und Veränderungen in der Umgebung eines Proteins sind bekannt dafür, potenziell Fehlfaltungen und Aggregation wie Amyloidbildung zu verursachen…”
Get full text
Journal Article -
6
Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approach
Published in PLoS computational biology (01-06-2012)“…Protein promiscuity is of considerable interest due its role in adaptive metabolic plasticity, its fundamental connection with molecular evolution and also…”
Get full text
Journal Article -
7
How many ionizable groups can sit on a protein hydrophobic core?
Published in Proteins, structure, function, and bioinformatics (01-01-2012)“…Full or partial burial of ionizable groups in the hydrophobic interior of proteins underlies the large modulation in group properties (modified pK value, high…”
Get full text
Journal Article -
8
Exploring Structural Determinants and Functional Aspects of Micron‐scale Protein Assemblies in Living Cells
Published in The FASEB journal (01-04-2020)“…Proteins are increasingly often seen as forming micron‐scale assemblies in their folded state. Such assemblies include, for example, CTP synthase, Glutamine…”
Get full text
Journal Article -
9
Not Going with the Flow: How Cells Adapt Internal Physics
Published in Cell (10-12-2020)“…Defining the principles underlying the organization of biomolecules within cells is a key challenge of current cell biology research. Persson et al. now…”
Get full text
Journal Article -
10
Proteins evolve on the edge of supramolecular self-assembly
Published in Nature (London) (10-08-2017)“…Introducing a single ‘sticky’ (hydrophobic) amino acid by point mutation into symmetric protein complexes frequently triggers their association into…”
Get full text
Journal Article -
11
Geometric description of self-interaction potential in symmetric protein complexes
Published in Scientific data (17-05-2019)“…Proteins can self-associate with copies of themselves to form symmetric complexes called homomers. Homomers are widespread in all kingdoms of life and allow…”
Get full text
Journal Article -
12
Proteins Evolve on the Edge of Supramolecular Self-Assembly
Published in Biophysical journal (03-02-2017)Get full text
Journal Article -
13
Infinite Ansammlungen gefalteter Proteine im Kontext von Evolution, Krankheiten und Proteinentwicklung
Published in Angewandte Chemie (16-04-2019)“…Mutationen und Veränderungen in der Umgebung eines Proteins sind bekannt dafür, potenziell Fehlfaltungen und Aggregation wie Amyloidbildung zu verursachen…”
Get full text
Journal Article