BIOMAT Database Logo BIOMAT Database Logo

Melting of the left-handed helical conformation of charged poly-L-lysine. 1994

A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.

UI MeSH Term Description Entries
D011107 Polylysine A peptide which is a homopolymer of lysine. Epsilon-Polylysine,Poly-(Alpha-L-Lysine),Epsilon Polylysine
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002151 Calorimetry The measurement of the quantity of heat involved in various processes, such as chemical reactions, changes of state, and formations of solutions, or in the determination of the heat capacities of substances. The fundamental unit of measurement is the joule or the calorie (4.184 joules). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
D002627 Chemistry, Physical The study of CHEMICAL PHENOMENA and processes in terms of the underlying PHYSICAL PHENOMENA and processes. Physical Chemistry,Chemistries, Physical,Physical Chemistries
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D017433 Protein Structure, Secondary The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D055598 Chemical Phenomena The composition, structure, conformation, and properties of atoms and molecules, and their reaction and interaction processes. Chemical Concepts,Chemical Processes,Physical Chemistry Concepts,Physical Chemistry Processes,Physicochemical Concepts,Physicochemical Phenomena,Physicochemical Processes,Chemical Phenomenon,Chemical Process,Physical Chemistry Phenomena,Physical Chemistry Process,Physicochemical Phenomenon,Physicochemical Process,Chemical Concept,Chemistry Process, Physical,Chemistry Processes, Physical,Concept, Chemical,Concept, Physical Chemistry,Concept, Physicochemical,Concepts, Chemical,Concepts, Physical Chemistry,Concepts, Physicochemical,Phenomena, Chemical,Phenomena, Physical Chemistry,Phenomena, Physicochemical,Phenomenon, Chemical,Phenomenon, Physicochemical,Physical Chemistry Concept,Physicochemical Concept,Process, Chemical,Process, Physical Chemistry,Process, Physicochemical,Processes, Chemical,Processes, Physical Chemistry,Processes, Physicochemical

Related Publications

A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Sodium trichloroacetate-induced helical conformation of poly(L-lysine).
August 1976, Biochimica et biophysica acta,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Left-handed helical conformation of poly[d(A-m5C).d(G-T)].
January 1983, Nature,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Left-handed double helical DNA: variations in the backbone conformation.
January 1981, Science (New York, N.Y.),
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Poly(epsilon-L-lysine): synthesis and conformation.
February 1980, Biopolymers,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Persistence length of α-helical poly-L-lysine.
September 2022, Soft matter,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Conformation of poly(L-lysine) homologs in solution.
April 1977, Biopolymers,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
A left-handed 3(1) helical conformation in the Alzheimer Abeta(12-28) peptide.
December 2003, FEBS letters,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
[Left-helical conformation (type poly-L-proline II) of the polypeptide chain of adrenocorticotropic hormone in water].
January 1976, Biofizika,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Conformational analysis of polynucleotides. I. The favorable left-handed helical model for the poly(8,2'-S-cycloadenylic acid) with high anti conformation.
August 1976, Nucleic acids research,
A A Makarov, and I A Adzhubei, and I I Protasevich, and V M Lobachov, and G D Fasman
Stability of the helical conformation of random L-alanine-L-lysine copolymers in aqueous solution.
January 1970, Biopolymers,
Copied contents to your clipboard!