Question

2. FILL IN THE BLANKS:

a) The ________ character of the peptide group limits the _____________ flexibility
of the polypeptide chain. The alpha helix and the beta sheet allow the polypeptide chain to adopt favorable ø and ⟒ ________ and to form _________ bonds. _________ proteins contain long stretches of regular secondary structure, such as the coiled coils in alpha __________ and the triple helix in ________. Not all polypeptides segments form regular ______________ structures such as alpha helices or beta sheets.

words:
​​​​​​​angles hydrogen fibrous hydrophobic collagen second polar tertiary nonpolar ionizing configurational high orientations bends planar disulfide hydrophilic globular conformational membrane-bound helix keratin hemoglobin myosin primary quaternary

b) The ___________ active Ser, ____ and Asp residues of serine proteases were identified by ________ labeling and structural analysis. A __________ pocket determines the substrate __________ of the various serine proteases. Serine __________ catalyze peptide bond hydrolysis via __________ and ____________ effects, acid-base catalysis, covalent catalysis, ____________ catalysis, and transition state _____________________. _______________ are the inactive precursors of _____________.


words: binding
active
holoenzymes
orientation
catalytically
antibody
hydrophobic
proteases
chemical
Apoenzymes
inhibition
proximity
electrostatic
energetically
metal ion
specificity
enzymes
global
Thr
stabilization
His
handedness
zymogens

Answer 1

a) The PLANAR character of the peptide bond limits the CONFORMATIONAL flexibility of the polypeptide chain. The alpha helix and beta sheet allows the polypeptide chain to adopt favourable psi and omega ANGLES to form HYDROGEN bonds. MEMBRANE bound proteins contain long stretches of secondary structures such as coiled coiled in alpha HELIX and triple helix in COLLAGEN. Not all polypeptides form regular SECONDARY structures such as alpha helix and beta sheets.

2. The CATALITICALLY active Serine, THR and asp residues of Serine proteases were identified by ANTIBODY labelling and structural analysis.A BINDING pocket determines the substrate SPECIFICITY of various Serine proteases. Serine PROTEASES catalyze peptide bond hydrolysis via PROXIMITY and ELECTROSTATIC effects, acid base catalysis,CHEMICAL catalysis and Transition state STABILIZATION. Zymogens are inactive precursors of ENZYMES.