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

Blankenship et al., 2002 - Google Patents

Probing backbone hydrogen bonds in the hydrophobic core of GCN4

Blankenship et al., 2002

Document ID
14575371766782552502
Author
Blankenship J
Balambika R
Dawson P
Publication year
Publication venue
Biochemistry

External Links

Snippet

Backbone amide hydrogen bonds play a central role in protein secondary and tertiary structure. Previous studies have shown that substitution of a backbone ester (− COO−) in place of a backbone amide (− CONH−) can selectively destabilize backbone hydrogen …
Continue reading at pubs.acs.org (other versions)

Classifications

    • 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
    • G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
    • 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
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • 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
    • 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
    • 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

Similar Documents

Publication Publication Date Title
Blankenship et al. Probing backbone hydrogen bonds in the hydrophobic core of GCN4
Du et al. Understanding the mechanism of β-hairpin folding via ϕ-value analysis
Struthers et al. Economy in protein design: Evolution of a metal-independent ββα motif based on the zinc finger domains
Isas et al. Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study
Kubelka et al. Discrimination between peptide 310-and α-helices. Theoretical analysis of the impact of α-methyl substitution on experimental spectra
Kuhlman et al. p K a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions
Eliezer et al. Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin
Lee et al. Fluorous effect in proteins: de novo design and characterization of a four-α-helix bundle protein containing hexafluoroleucine
Kobayashi et al. Role of Side-chains in the Cooperative β-Hairpin Folding of the Short C− Terminal Fragment Derived from Streptococcal Protein G
Apostolovic et al. pH-sensitivity of the E3/K3 heterodimeric coiled coil
Tucker et al. Conformational distribution of a 14-residue peptide in solution: A fluorescence resonance energy transfer study
Gauba et al. Surprisingly high stability of collagen ABC heterotrimer: evaluation of side chain charge pairs
Reiner et al. Effect of thioxopeptide bonds on α-helix structure and stability
Searle et al. Energetics of weak interactions in a β-hairpin peptide: Electrostatic and hydrophobic contributions to stability from lysine salt bridges
Woll et al. Backbone thioester exchange: A new approach to evaluating higher order structural stability in polypeptides
Starzyk et al. Spectroscopic evidence for backbone desolvation of helical peptides by 2, 2, 2-trifluoroethanol: an isotope-edited FTIR study
Yoder et al. Characterization of alanine-rich peptides, Ac-(AAKAA) n-GY-NH2 (n= 1− 4), using vibrational circular dichroism and Fourier transform infrared. Conformational determination and thermal unfolding
Kuhlman et al. Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding
Love et al. The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA
Kaul et al. Incorporating β-turns and a turn mimetic out of context in loop 1 of the WW domain affords cooperatively folded β-sheets
Setnička et al. IR study of cross-strand coupling in a β-hairpin peptide using isotopic labels
Beligere et al. Design, synthesis, and characterization of 4-ester CI2, a model for backbone hydrogen bonding in protein α-helices
Hudáky et al. Cooperation between a salt bridge and the hydrophobic core triggers fold stabilization in a Trp-cage miniprotein
Riemen et al. Design of highly stabilized β-hairpin peptides through cation− π interactions of lysine and n-methyllysine with an aromatic pocket
Weiss et al. Hierarchical Protein “Un-Design”: Insulin's Intrachain Disulfide Bridge Tethers a Recognition α-Helix