serw-MX  [xml]  

 DeCS Categories

G02 Chemical Phenomena .
G02.111 Biochemical Phenomena .
G02.111.570 Molecular Structure .
G02.111.570.820 Molecular Conformation .
G02.111.570.820.709 Protein Conformation .
G02.111.570.820.709.600 Protein Structure, Secondary .
G02.111.570.820.709.600.750 Protein Conformation, beta-Strand .
G02.111.570.820.709.610 Protein Structure, Tertiary .
G05 Genetic Phenomena .
G05.360 Genetic Structures .
G05.360.340 Genome .
G05.360.340.024 Genome Components .
G05.360.340.024.340 Genes .
G05.360.340.024.340.610 Major Histocompatibility Complex .
G05.360.340.024.380 Genetic Loci .
G05.360.340.024.380.500 Major Histocompatibility Complex .
G12 Immune System Phenomena .
G12.500 Immunogenetic Phenomena .
G12.500.500 Major Histocompatibility Complex .
I01 Social Sciences .
I01.240 Demography .
I01.240.425 Health Status .
N01 Population Characteristics .
N01.224 Demography .
N01.224.425 Health Status .
N06 Environment and Public Health .
N06.850 Public Health .
N06.850.505 Epidemiologic Measurements .
N06.850.505.400 Demography .
N06.850.505.400.425 Health Status .
SP5 Epidemiology and Biostatistics .
SP5.001 Epidemiology .
SP5.001.047 Uses of Epidemiology .
SP5.001.047.103 Diagnosis of Health Situation .
SP5. Health Status .
 Synonyms & Historicals
Protein Structure, Secondary .
Secondary Protein Structure .
Protein Structures, Secondary .
Secondary Protein Structures .
Structure, Secondary Protein .
Structures, Secondary Protein .
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. .
Protein Structure, Tertiary .
Tertiary Protein Structure .
Protein Structures, Tertiary .
Tertiary Protein Structures .
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. .
Health Status .
Health Level .
Health Levels .
Status, Health .
Level of Health .
Health Conditions .
The level of health of the individual, group, or population as subjectively assessed by the individual or by more objective measures. .
Major Histocompatibility Complex .
Complex, Histocompatibility .
Complex, Major Histocompatibility .
Complices, Histocompatibility .
Complices, Major Histocompatibility .
Histocompatibility Complex, Major .
Histocompatibility Complices .
Histocompatibility Complices, Major .
Major Histocompatibility Complices .
Histocompatibility Complex .
The genetic region which contains the loci of genes which determine the structure of the serologically defined (SD) and lymphocyte-defined (LD) TRANSPLANTATION ANTIGENS, genes which control the structure of the IMMUNE RESPONSE-ASSOCIATED ANTIGENS, HUMAN; the IMMUNE RESPONSE GENES which control the ability of an animal to respond immunologically to antigenic stimuli, and genes which determine the structure and/or level of the first four components of complement. .
Protein Conformation, beta-Strand .
beta-Pleated Sheet .
beta-Sheet .
beta-Sheets .
beta-Strand .
beta-Stranded Structures .
beta-Strands .
Conformation, beta-Sheet Protein .
Conformation, beta-Strand Protein .
Conformations, beta-Sheet Protein .
Conformations, beta-Strand Protein .
Protein Conformation, beta Sheet .
Protein Conformation, beta Strand .
Protein Conformations, beta-Sheet .
Protein Conformations, beta-Strand .
Sheet, beta-Pleated .
Sheets, beta-Pleated .
beta Pleated Sheet .
beta Sheet .
beta Sheets .
beta Strand .
beta Stranded Structures .
beta Strands .
beta-Pleated Sheets .
beta-Sheet Protein Conformation .
beta-Sheet Protein Conformations .
beta-Strand Protein Conformation .
beta-Strand Protein Conformations .
beta-Stranded Structure .
Protein Conformation, beta-Sheet .
A secondary structure of proteins where the amino (N-H) groups of a polypeptide backbone, three to ten amino acids in length, establish hydrogen bonds with the carbonyl (C=O) groups in the backbone of adjacent strands. These may form a beta-sheet, where the side chains of the adjacent strands point in the same direction. .