Effect of disorganization of carbohydrate-protein complexes of the ground substance on structure and physicochemical properties of human hyaline cartilage

1991 ◽  
Vol 111 (3) ◽  
pp. 330-333 ◽  
Author(s):  
V. A. Dubinskaya ◽  
S. S. Nikolaeva ◽  
Yu. A. Khoroshkov ◽  
O. A. Koroleva
Keyword(s):  
Physicochemical Properties ◽  
Hyaline Cartilage ◽  
Protein Complexes ◽  
Ground Substance ◽  
Human Hyaline Cartilage

Structural effects in chemistry and biology

2000 ◽  
Vol 04 (04) ◽  
pp. 382-385 ◽  
Author(s):  
JACK FAJER
Keyword(s):  
Excited State ◽  
Physicochemical Properties ◽  
Crystal Structures ◽  
Protein Complexes ◽  
Structural Effects ◽  
Conformational Variations ◽  
Prosthetic Groups ◽  
Skeletal Deformations

Conformationally designed, non-planar porphyrins afford new classes of structurally distinct chromophores with significantly altered optical, redox, magnetic, radical and excited state properties. The synthetic, non-planar porphyrins model and illustrate the consequences of the skeletal deformations and plasticity increasingly observed in crystal structures of protein complexes comprising porphyrinic chromophores and prosthetic groups. Conformational variations thus offer attractively simple mechanisms for modulating the physicochemical properties of porphyrins in vivo and in vitro.

A system of interlacunar network and thick fibrils in human hyaline cartilage

1990 ◽  
Vol 22 (4) ◽  
pp. 201-208 ◽  
Author(s):  
W. S. Hwang ◽  
J. Hugh ◽  
K. Ngo
Keyword(s):  
Hyaline Cartilage ◽  
Human Hyaline Cartilage

New thermogravimetric protocol for the investigation of normal and damaged human hyaline cartilage

2007 ◽  
Vol 89 (3) ◽  
pp. 853-856 ◽  
Author(s):  
G. Sohár ◽  
E. Pallagi ◽  
P. Szabó-Révész ◽  
K. Tóth
Keyword(s):  
Hyaline Cartilage ◽  
Human Hyaline Cartilage

Human hyaline cartilage — biochemical and immunochemical study

1987 ◽  
Vol 82 (2) ◽  
pp. 185-191
Author(s):  
Mária Ružičková ◽  
Eva Surmíková ◽  
Miroslav Brozman
Keyword(s):  
Hyaline Cartilage ◽  
Immunochemical Study ◽  
Human Hyaline Cartilage

Novel calorimetric investigation of different degenerative disorders of the human hyaline cartilage

2009 ◽  
Vol 95 (3) ◽  
pp. 801-804 ◽  
Author(s):  
Z. Aigner ◽  
L. Mécs ◽  
G. Sohár ◽  
K. Wellinger ◽  
Piroska Szabó-Révész ◽  
...  
Keyword(s):  
Hyaline Cartilage ◽  
Calorimetric Investigation ◽  
Human Hyaline Cartilage ◽  
Degenerative Disorders

scholarly journals 453 COMPARING PHYSICAL PROPERTIES OF OSTEOARTHRITIC AND NECROTIC HUMAN HYALINE CARTILAGE

2008 ◽  
Vol 16 ◽  
pp. S196-S197
Author(s):  
G. Sohár ◽  
Z. Aigner ◽  
P. Szabó-Révész ◽  
K. Tóth
Keyword(s):  
Physical Properties ◽  
Hyaline Cartilage ◽  
Human Hyaline Cartilage

Formation of in vivo tissue engineered human hyaline cartilage in the shape of a trachea with internal support

2005 ◽  
Vol 69 (11) ◽  
pp. 1489-1495 ◽  
Author(s):  
Binti Haji Idrus Ruszymah ◽  
Kienhui Chua ◽  
Mazlyzam Abdul Latif ◽  
Fuzina Nor Hussein ◽  
Aminuddin Bin Saim
Keyword(s):  
Hyaline Cartilage ◽  
Human Hyaline Cartilage ◽  
Internal Support

scholarly journals Mutants libraries reveal negative design shielding proteins from mis-assembly and re-localization in cells

2021 ◽  
Author(s):  
Hector Garcia Seisdedos ◽  
Tal Levin ◽  
Gal Shapira ◽  
Saskia Freud ◽  
Emmanuel Levy
Keyword(s):  
Physicochemical Properties ◽  
Protein Complexes ◽  
Internal Symmetry ◽  
Yeast Cells ◽  
Net Charge ◽  
Protein Surfaces ◽  
Oligomeric Protein ◽  
Cellular Context ◽  
And Function ◽  
The Impact

ABSTRACTUnderstanding the molecular consequences of mutations in proteins is essential to map genotypes to phenotypes and interpret the increasing wealth of genomic data. While mutations are known to disrupt protein structure and function, their potential to create new structures and localization phenotypes has not yet been mapped to a sequence space. To map this relationship, we employed two homo-oligomeric protein complexes where the internal symmetry exacerbates the impact of mutations. We mutagenized three surface residues of each complex and monitored the mutations’ effect on localization and assembly phenotypes in yeast cells. While surface mutations are classically viewed as benign, our analysis of several hundred mutants revealed they often trigger three main phenotypes in these proteins: nuclear localization, the formation of puncta, and fibers. Strikingly, more than 50% of random mutants induced one of these phenotypes in both complexes. Analyzing the mutant’s sequences showed that surface stickiness and net charge are two key physicochemical properties associated with these changes. In one complex, more than 60% of mutants self-assembled into fibers. Such a high frequency is explained by negative design: charged residues shield the complex from misassembly, and the sole removal of the charges induces its assembly. A subsequent analysis of several other complexes targeted with alanine mutations suggested that negative design against mis-assembly and mislocalization is common. These results highlight that minimal perturbations in protein surfaces’ physicochemical properties can frequently drive assembly and localization changes in a cellular context.

Sign in / Sign up

Export Citation Format

Share Document