Preferred Label : protein structure, tertiary;
MeSH definition : The level of protein structure in which combinations of secondary protein structures
(alpha helices, beta sheets, loop regions, and motifs) pack together to form folded
shapes called domains. Disulfide bridges between cysteines in two different parts
of the polypeptide chain along with other interactions between the chains play a role
in the formation and stabilization of tertiary structure. Small proteins usually consist
of only one domain but larger proteins may contain a number of domains connected by
segments of polypeptide chain which lack regular secondary structure.; The level of protein structure in which combinations of secondary protein structures
(ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to
form folded shapes. Disulfide bridges between cysteines in two different parts of
the polypeptide chain along with other interactions between the chains play a role
in the formation and stabilization of tertiary structure.;
MeSH synonym : tertiary protein structure; protein structures, tertiary; tertiary protein structures;
CISMeF synonym : domain, peptide; peptide domains; domain, protein; domains, protein; protein domain; peptide domain; domains, peptide;
MeSH annotation : IM general; coord NIM with specific protein (IM); PROTEIN MOTIFS see MOTIFS, AMINO
ACID is available; IM general only; coordinate NIM with specific protein;
Origin ID : D017434;
UMLS CUI : C0162808;
Allowable qualifiers
- Automatic exact mappings (from CISMeF team)
- Currated CISMeF NLP mapping
- Record concept(s)
- See also inter- (CISMeF)
- Semantic type(s)
- UMLS correspondences (same concept)
The level of protein structure in which combinations of secondary protein structures
(alpha helices, beta sheets, loop regions, and motifs) pack together to form folded
shapes called domains. Disulfide bridges between cysteines in two different parts
of the polypeptide chain along with other interactions between the chains play a role
in the formation and stabilization of tertiary structure. Small proteins usually consist
of only one domain but larger proteins may contain a number of domains connected by
segments of polypeptide chain which lack regular secondary structure.
The level of protein structure in which combinations of secondary protein structures
(ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to
form folded shapes. Disulfide bridges between cysteines in two different parts of
the polypeptide chain along with other interactions between the chains play a role
in the formation and stabilization of tertiary structure.
