BS1005 Lab Report two

 BS1005 Lab Report two Essay

SCHOOL OF BIOLOGICAL SAVOIR

BS1005 BIOCHEMISTRY AND BIOLOGY 1

Brand: Kingston Suntan Lee Kang

Matriculation Amount: U1440619E

Tutorial Group: 8

LAB SURVEY

Practical 2- Macromolecule Composition Study

Institution of Neurological Science, NTU

BS1005 Useful: Macromolecule Structure Study

Outcomes & Discourse on Problems

Peptide I – PDB I (β – Sheet)

Determine 1 . ‘Cartoon view' of Peptide I actually showing their secondary composition

Figure one particular illustrates the secondary framework of PDB file 1 which displays a β – Linen. 3 hydrogen bond relationships between a great amide and oxygen group were identified. The 3 sets of residues that hydrogen bonds had been formed among were identified and proven below in Figure 2 . Bond ranges and connection angles were identified. (Bond distance – Coloured green, Bond position – Girl yellow)

Number 2 . Composition of Peptide I with residues with the bond perspectives & connection distances

Residues involved in the

hydrogen bond

LEU-144 & TYR 137

LEU-146 & VAL-135

TYR-148 & ILE-133

Connect Distance (Г…)

Bond Perspective (o)

2 . 07

1 . 86

1 . 92

158. 99

161. 49

159. 80

Table 1 . Relationship distance & Bond aspects between hydrogen bonds

Page 1

College of Biological Science, NTU

BS1005 Functional: Macromolecule Composition Study

Determine 3. Phi & Pound-force per square inch angles for peptide We

Residue of Peptide My spouse and i

ILE-133

TYR-148

VAL-135

LEU-146

TYR-137

LEU-144

Phi П† angle(o)

-131. 35

-135. 47

-137. 77

-141. 99

-146. 03

-111. 41

Pound-force per square inch П€ angle(o)

134. forty

122. 82

132. forty-nine

135. 41

126. 49

140. 98

Table 2 . Phi П† angle & Psi П€ angle for Peptide My spouse and i

As discovered from Figure 3, calculation of central source torsion position of residues (Coloured orange) was performed via the way of measuring function of PyMOL and recorded in the table seen above.

As illustrated in Determine 1, Peptide 1 is usually observed to have an anti-parallel β – Linens based on the visualized second structure whereby strands are seen to be moving in opposite guidelines. Furthermore, Desk 1 provides further information to shows that the moment residues coming from 1 of the β – Linen increases in residue quantity, the other β – Sheet has a decrease in residue number. Which in turn also helps with showing the β – Sheets strands moving in distinct direction. Peptide II – PDB a couple of (α – Helix & β – Sheet)

Physique 3. ‘Cartoon view' of Peptide II showing their secondary framework

Page a couple of

School of Biological Technology, NTU

BS1005 Practical: Macromolecule Structure Research

α – Helix

Figure 4. Peptide II (α – Helix Structure) with residues using their bond perspectives & relationship distances

Figure 4 illustrates the hydrogen bond communications within the α – Helix structure from the peptide II. The elements are demonstrated above mentioned by the girl lines (Bond distance – Coloured green, Bond angle – Girl yellow). Relationship distances & bond sides are proven in the table below.

Residues involved in the hydrogen bond

MET-878 & LEU-882

ALA-881 & HIS-884

LEU-882 & MET-885

Bond Range (Г…)

1 . 92

installment payments on your 06

2 . 38

Relationship Angle (o)

161. 18

147. twenty-two

170. 87

Table a few. Bond range & Bond angles among hydrogen you possess

Figure a few. Peptide II (α – Helix Structure) - Phi & Pound-force per square inch (psi) angles

Residue of Peptide II (α – Helix Structure)

MET-878

LEU-882

MET-885

ALA-881

HIS-884

Phi П† angle(o)

-65. 90

-59. 01

-66. 64

-58. 91

-117. 92

Pound-force per square inch П€ angle(o)

-36. 02

-39. eighty six

-3. 90

-50. twenty-two

11. 83

Table 5. Phi φ angle & Psi ψ angle intended for Peptide 2 (α – Helix Structure)

Page three or more

School of Biological Scientific research, NTU

BS1005 Practical: Macromolecule Structure Analyze

As observed from Physique 5, calculations of anchor torsion viewpoint of elements (Coloured orange) was carried out via the dimension function of PyMOL and recorded inside the table seen the pictures.

β – Sheet

Determine 6. Peptide II (β – Sheet) with residues with their relationship angles & bond miles

Figure 5 illustrates the hydrogen connect interactions within the β – Sheet structure of the peptide II. The residues will be shown previously mentioned indicated by the coloured lines (Bond length – Female blue, Relationship angle – Coloured...


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