Nothing Special   »   [go: up one dir, main page]

Gauba et al., 2007 - Google Patents

Surprisingly high stability of collagen ABC heterotrimer: evaluation of side chain charge pairs

Gauba et al., 2007

Document ID
648026736731265137
Author
Gauba V
Hartgerink J
Publication year
Publication venue
Journal of the American Chemical Society

External Links

Snippet

Type I collagen is a major component of skin, tendon, and ligament and forms more than 90% of bone mass. It is an AAB heterotrimer assembled from two identical α1 and one α2 chains. However, the majority of studies on the effects of amino acid substitution on triple …
Continue reading at pubs.acs.org (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
    • C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
    • C07K1/1136—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/001—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof by chemical synthesis
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
    • C07K1/1072—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/14—Extraction; Separation; Purification
    • C07K1/16—Extraction; Separation; Purification by chromatography
    • C07K1/22—Affinity chromatography or related techniques based upon selective absorption processes

Similar Documents

Publication Publication Date Title
Gauba et al. Surprisingly high stability of collagen ABC heterotrimer: evaluation of side chain charge pairs
Sarkar et al. Self-assembly of fiber-forming collagen mimetic peptides controlled by triple-helical nucleation
Gauba et al. Self-assembled heterotrimeric collagen triple helices directed through electrostatic interactions
Yu et al. Minimal lipidation stabilizes protein-like molecular architecture
Rele et al. D-periodic collagen-mimetic microfibers
Reiner et al. Effect of thioxopeptide bonds on α-helix structure and stability
Apostolovic et al. pH-sensitivity of the E3/K3 heterodimeric coiled coil
Persikov et al. Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability
Tao et al. Self-assembly of short Aβ (16− 22) peptides: Effect of terminal capping and the role of electrostatic interaction
Acharya et al. Stability of 100 homo and heterotypic coiled− coil a− a ‘pairs for ten amino acids (A, L, I, V, N, K, S, T, E, and R)
Melnyk et al. Retention of native-like oligomerization states in transmembrane segment peptides: application to the Escherichia coli aspartate receptor
Li et al. Sequence directionality dramatically affects LCST behavior of elastin-like polypeptides
Chin et al. Gas phase formation of a 310-helix in a three-residue peptide chain: role of side chain-backbone interactions as evidenced by IR− UV double resonance experiments
Lear et al. Position-dependence of stabilizing polar interactions of asparagine in transmembrane helical bundles
Nishi et al. Different effects of 4-hydroxyproline and 4-fluoroproline on the stability of collagen triple helix
Gokce et al. Single peptide bonds exhibit poly (pro) II (“random coil”) circular dichroism spectra
Gunasekar et al. N-terminal aliphatic residues dictate the structure, stability, assembly, and small molecule binding of the coiled-coil region of cartilage oligomeric matrix protein
O’Leary et al. Positive and negative design leads to compositional control in AAB collagen heterotrimers
Kessler et al. Peptoid residues make diverse, hyperstable collagen triple-helices
Naduthambi et al. Stereoelectronic tuning of the structure and stability of the trp cage miniprotein
Egli et al. Influence of lipidation on the folding and stability of collagen triple helices—an experimental and theoretical study
Condon et al. Development of a coarse-grained model of collagen-like peptide (CLP) for studies of CLP triple helix melting
Liu et al. Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease
Li et al. Covalent Capture of a Heterotrimeric Collagen Helix
Blankenship et al. Probing backbone hydrogen bonds in the hydrophobic core of GCN4